СОДЕРЖАЩИЕ ГАЛАКТОЗА-АЛЬФА-1,3-ГАЛАКТОЗУ N-ГЛИКАНЫ В ГЛИКОПРОТЕИНОВЫХ ПРОДУКТАХ, ПОЛУЧЕННЫХ ИЗ КЛЕТОК СНО

... 1. Способ оценки популяции клеток яичника китайского хомячка (СНО), включающий:(a) обеспечение одной или более клеток СНО из популяции; и(b) измерение гликанов, содержащих терминальные остатки галактоза-альфа-1-3-галактозы, продуцированные указанными клетками, где клетки СНО не были генетически сконструированы, чтобы экспрессировать последовательность, кодирующую альфа-галактозилтрансферазу.2. Способ по п.1, где этап измерения включает любое из следующих:(a) выделение гликопротеинов, продуцированных из клеток СНО, и измерение гликанов, содержащих терминальные остатки галактоза-альфа-1-3-галактозы на гликопротеинах,(b) выделение специфической гликопротеиновой композиции, продуцированной из клеток СНО, и измерение гликанов, содержащих терминальные остатки галактоза-альфа-1-3-галактозы, из композиции выделенных гликопротеинов,(c) получение гликанового препарата из гликопротеинового препарата или выделенного гликопротеина, продуцированного из клеток СНО, и измерение гликанов, содержащих терминальные ...

An antibody, a biomonitoring kit and method

An antibody for use in a biomonitoring test using enzyme-linked immunosorbent assay, a kit for carrying out the test and a method of carrying out the test. More particularly the antibody is a primary antibody which is labelled with an enzyme and is used to determine a person's exposure to one of: benzene; polycyclic aromatic hydrocarbons; isocyanates; ethylene oxide; or propylene oxide.

A method of isolating exosomes

INTERMEDIATE CONNECTIONS OF ADVANCED GLYKOSYLIERUNG FINAL PRODUCTS AND POST OFFICE AMADORI INHIBITOR

Antibodies, pharmaceutical compositions and uses thereof

The present invention provides antibodies or the antigen-binding portion thereof, that bind to one or more carbohydrate antigens. Also disclosed herein are pharmaceutical pharmaceutical compositions and methods for the inhibition of cancer cells in a subject in need thereof. The pharmaceutical compositions comprise an antibody or an antigen binding portion thereof and at least one pharmaceutically acceptable carrier.

Galactose-alpha-1, 3-galactose-containing N-glycans in glycoprotein products derived from CHO cells

The present invention provides methods for evaluating a Chinese Hamster Ovary (CHO) cell population by measuring glycans containing terminal galactose-alpha-1-3-galactose residues produced by said cells, wherein the CHO cells have not been genetically engineered to express an alpha-galactosyl transferase coding sequence.

SYNTHETIC OLIGOSACCHARIDE SUBUNITS OF THE PSL EXOPOLYSACCHARIDE OF PSEUDOMONAS AERUGINOSA AND USES THEREOF

This disclosure relates to synthetic oligosaccharide subunits of the Pseudomonas exosaccharide Psl and uses thereof, e.g, for epitope mapping of anti-Psl antibodies, for identification of anti-Psl antibodies, and for use as vaccines.

Means and methods for glycoprofiling of a protein

The present invention provides magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon including uses in methods for glycoprofiling of glycoproteins using lectins, e.g., in diagnostics of cancer. The magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein.

ASSAY FOR GLYCOSYLATED PROTEINS

The invention provides a method for assaying for a protein having at least two isoforms having different glycosylation patterns, said method comprising: contacting a sample containing said protein with a carbohydrate-binding agent and a ligand capable of binding to at least two said isoforms, and detecting conjugates of said carbohydrate-binding agent and said protein and/or of said ligand and said protein.

METHOD OF DETECTING SACCHARIFIED ALBUMIN

To quantify saccharified albumin, it is intended to provide a means of giving quantification data, which correlate to the data of the quantification of saccharified albumin by the HPLC method, without giving any intercept which might disturb the use in clinical medicine in case where regression formula is plotted by using the corrective quantification method with the use of enzymes. Namely, a method of detecting saccharified albumin in the serum by using a reagent for assaying fructosamine, which comprises using a reagent for assaying saccharified proteins by quantifying saccharified proteins in the serum, correcting the value by dividing the thus obtained value by the total albumin content in the serum and referring the thus corrected value as the saccharified albumin content in the serum, wherein use is made, as a saccharified albumin standard, of saccharified albumin obtained from human blood by subjecting an albumin fraction originating in the blood of a normal subject to a treatment ...

CAMPYLOBACTER GLYCANS AND GLYCOPEPTIDES

Multiple strains and species of Campylobacter were found to share a common glycan moitie which is present in a plurality of surface-exposed glycoproteins. This glycan has the formula: GalNAc-a1,4-GalNAc-a1,4-[Glc- .szlig.1,3]GalNAc-a1,4-GalNAc-a1,4-GalNAc-a1,3-Bac, wherein Bac is 2,4- diacetamido-2,4,6-trideoxy-D-glucopyranose. This glycan and immunologically active fragments of it have use as vaccines against campylobacter infection in humans and animals. As well, antibodies which specifically bind these compounds may be provided. Such antibodies and vaccines may be used to prevent or neutralize campylobacter infections in livestock thereby preventing this pathogen from entering the human food chain. The glycan may be linked to one or more amino acids to form a glycopeptide. As well, a method for determining the glycan structure of an intact glycoprotein consists of subjecting a sample to high resolution magic angle spinning nuclear magnetic resonance (HR-MAS- NMR) spectroscopy.

STEROL GLUCOSIDES IN DISEASE

The etiology of various age-related neurological diseases remains unknown. Sporadic forms of Alzheimer's, Parkinson's, and Lou Gehrig's disease have been linked to environmental factors that cause neuronal cell death by either by excitotoxicity or by inducing oxidative stress. Our recent studies have demonstrated that various compounds not previously associated with these diseases, i.e., methionine sulfoximine and sitosterol glucoside, appear to be neurotoxins, likely acting by excitotoxic mechanisms. For these compounds, the primary excitotoxic effect appears to involve glutamate release followed by NMDA receptor activation. Lactate dehydrogenase assays demonstrate that both compounds cause rapid cell death in vitro. In addition, both compounds appear to alter antioxidant defense mechanisms, acting particularly on levels of reduced glutathione (GSH). In vivo application of MSO has historically been linked to behavioral abnormalities, including seizures, in various species. Our recent experiments ...

A-FUCOSYLATION DETECTION IN ANTIBODIES

This invention describes a new analytical method to determine the quantity and distribution of fucose per Fc within an antibody preparation.

STEROL GLUCOSIDE TOXINS

The invention relates to the identification of sterol glucoside toxins, and provides methods for detecting and detoxifying the compounds, as well as therapeutic methods for treating subjects exposed to such toxins. In alternative embodiments, the toxins may for example include beta-sitostrol- beta-D-glucoside (5-cholesten-24b-ethyl-3b-ol-D-glucoside) or cholesterol glucoside (5-cholesten-3b-ol-3b-D-glucoside).

ANTIBODIES, PHARMACEUTICAL COMPOSITIONS AND USES THEREOF

MELANOTRANSFERRIN FOR USE IN THE DIAGNOSIS OF PARKINSON`S DISEASE

The present invention is the protein of melanotransferrin, or an encoding nucleic acid of same, for use in the diagnosis of Parkinson's disease (PD). The invention is a method of diagnosis of PD in a subject, comprising assessing the level of melanotransferrin in the saliva or in a saliva sample of said subject and determining whether said level is above or below a value of 8.6 µg/ml, wherein a value below 8.6 µg/ml is indicative of PD. Another aspect is a kit comprising at least one reagent, preferably an antibody, for the quantification of melanotransferrin in the saliva or in a saliva sample of a subject enabling the comparison of said quantification with a predetermined cut-off value.

METHOD OF REMOVING ADHESIVE MICROVESICLES

PANCREATIC CANCER DETECTION METHOD

In order to provide a pancreatic cancer detection method, and more specifically a pancreatic cancer detection method capable of determining even earlier-stage pancreatic cancer, this method for detecting the possibility of pancreatic cancer morbidity involves (1) a step in which the amount, in a biological sample extracted from a subject, of at least one type of anti-sugar chain antibody is measured, selected from the group consisting of an anti-3-sialyllactose carbohydrate antibody and an anti-(LN) 3-sugar chain antibody, wherein the anti-3-sialyllactose carbohydrate antibody is an antibody that can bond to a sugar chain represented by Neu5Aca(2?3)Galß(1?4)Glc, or an antibody that recognizes said sugar chain, and the anti-(LN) 3-sugar chain antibody is antibody that can bond to a sugar chain represented by Galß1?3GlcNAcß1?3Galß1?4GlcNAc, or an antibody that recognizes said sugar chain.

BIOMARKERS FOR PROSTATE CANCER AND METHODS FOR THEIR DETECTION

The invention provides a method for predicting the clinical response to a cancer vaccine in a patient having cancer, a method for determining the immune response to a cancer vaccine in a patient having cancer who has been administered a cancer vaccine, a method for determining the long-term survival in a patient having cancer, corresponding kits therefor, as well as methods of for improving the efficacy of a virus-based vaccine.

METHOD FOR ANALYZING MUCIN 1 USING PROBE CAPABLE OF BINDING TO 3´ SULFONATED CORE 1 CARBOHYDRATE CHAIN, AND METHOD FOR DETECTING OR MONITORING BREAST CANCER

The purpose of the present invention is to provide a method for detecting even mucin 1 derived from breast cancer, which cannot be detected by a CA15-3 measurement method. The purpose can be achieved by a method for analyzing mucin 1 having a Sulfo-3Galß1-3GalNAc-R carbohydrate chain, characterized by comprising: a step of bringing a 3´-sulfonated core 1 carbohydrate chain binding probe capable of binding to the Sulfo-3Galß1-3GalNAc-R carbohydrate chain into contact with a sample to be tested; a step of bringing a 3´-sulfonated core 1 carbohydrate chain mucin 1 peptide binding probe capable of binding to mucin 1 having the Sulfo-3Galß1-3GalNAc-R carbohydrate chain or a mucin 1 binding probe capable of binding to mucin 1 into contact with the sample; and a step of detecting a bonded product of mucin 1 having the Sulfo-3Galß1-3GalNAc-R carbohydrate chain and the probes.

C-ERBB-2 EXTERNAL DOMAIN:GP75

Disclosed are methods and compositions for identifying malignant tumors that overexpress the c-erbB-2 oncogene. Assays useful for diagnosis and prognosis of neoplastic disease are provided which detect the external domain of c-erbB-2, the glycoprotein gp75 and quantitate the level of gp75 in the biological fluids of mammals carrying a tumor burden. Further disclosed are recombinant, synthetically and otherwise biologically produced novel proteins and polypeptides which are encoded by the external domain DNA sequence of the c-erbB-2 oncogene (the gp75 gene) or fragments thereof. Such gp75 proteins and polypeptides are useful as vaccines, therapeutically in the treatment of cancer either alone or in combination with chemotherapeutic agents. Also disclosed are antibodies to such gp75 proteins and polypeptides which are useful diagnostically and therapeutically. Still further disclosed are test kits embodying the assays of this invention.

LECTIN-BASED GLYCAN ASSAY

The invention relates to the use of deglycosylated detectors, especially secondary antibodies, for determination of the sugar structures of proteins, especially recombinant proteins. It further relates especially to the use of deglycosylated enzymes in the determination of sugar structures with the aid of an enzyme-substrate reaction; the invention further relates to a process for determining the sugar structures of proteins, and to a sugar determination kit, and to the use of the kit for determining sugar structures, especially recombinant therapeutic proteins, preferably immunoglobulins.

METHOD OF SCREENING FOR CANCER AND ADENOMA

... [PROBLEMS] To provide a method of screening, and a test agent, capable of detecting cancer patients and patients with a high risk of cancer at high percentage. [MEANS FOR SOLVING PROBLEMS] A remarkable difference in the distribution of sugar chain sulfating enzyme GlcNAc-6-sulfotransferase isozymes has been found between noncancerous tissues and cancer/adenoma tissues. By the use of the same, it has been clarified that cancer and adenoma (excluding colon cancer and colon adenoma) can be specifically detected through detection of a given range of GlcNAc-6-sulfated sugar chains from patient tissues or fecal specimens. Cancer and adenoma screening can be carried out by the use of an antibody capable of reacting with GlcNAc-6-sufated sugar chains specifically formed by enzymes occurring in cancer and adenoma tissues.

METHOD OF REMOVING ADHESIVE MICROVESICLES

A method whereby microvesicles released from platelets, which have been activated by an artificial procedure in pre-treating a blood-origin sample with albumin, are exclusively removed and microvesicles in the blood alone are measured.

METHODS, PRODUCTS AND TREATMENTS FOR DIABETES

The invention involves assays, diagnostics, kits, and assay components for determining levels of K41-glycated CD59 in subjects. Treatments for subjects based upon levels of K41-glycated CD59 also are provided.

Monoclonal antibody reacting with glycopeptide, and use thereof

Disclosed is a monoclonal antibody reacting with a glycopeptide, wherein the glycopeptide contains a core fucose moiety and at least 4 contiguous amino acid residues that are located on the C-terminal side of a glycosylated asparagine moiety, and both of the core fucose moiety in the glycopeptide and an amino acid residue that is located apart by at least three amino acid residues from the C-terminal of the glycosylated asparagine moiety in the glycopeptide are epitopes for the antibody.

Method of detecting cancer based on glycan biomarkers

The present invention provides a method for labeling or detecting a protein with certain glycosyl groups. The methods are particularly useful for detecting cancer cells comprising the detected glycosyl groups. The present invention further provides labeling agents and detection agents, labeled proteins and mixtures, and kits and arrays thereof.

Methods and compositions for measuring natriuretic peptides and uses thereof

The present invention describes compositions and methods designed to determine the presence or amount of natriuretic peptides, or their fragments, in a sample. The degradation of natriuretic peptides is an ongoing process that may be a function of, inter alia, the elapsed time between onset of an event triggering natriuretic peptide release into the tissues and the time the sample is obtained or analyzed; the quantity of proteolytic enzymes present; etc. This degradation can produce circulating amounts of natriuretic peptides having reduced or lost biological function. The present invention provides, inter alia, assays designed to accurately measure biologically active natriuretic peptides, and compositions to inhibit a previously unknown pathway for degradation of natriuretic peptides.

Compositions and Methods to Inhibit Estrogen Receptor Beta for the Treatment of Renal Cell Carcinoma

The invention provides compositions and methods for treating and preventing cancer. The invention relates to compositions and methods for treating subjects having a cancer associated with overexpression of estrogen receptors, especially in males. The invention comprises inhibitors of ERβ, inhibitors of TGFβ-1, inhibitors of SMAD, or inhibitors of HIF, or a combination thereof. In one embodiment, the invention provides a method of treating renal cancer, including renal cell carcinoma.

CARBOHYDRATE LIGANDS THAT BIND TO IGM ANTIBODIES AGAINST MYELIN-ASSOCIATED GLYCOPROTEIN

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone.

METHOD OF REMOVING ADHESIVE MICROVESICLES

A method for selectively measuring microvesicles alone in blood by pretreating a sample derived from blood with albumin to selectively eliminate microvesicles alone released from platelets activated by an artificial manipulation.

Medical utility of glycans

The present invention relates to the use of glycan-binding polypeptides and glycans as a medicament, in particular for treating and/or preventing helminthic infections or an immune disease. Moreover, the present invention is directed to corresponding pharmaceutical compositions, food products and animal feed comprising isolated glycans and/or glycan-binding polypeptides. In addition, the present invention teaches methods for identifying anti-helminthic carbohydrate-binding polypeptides, for identifying helminthic glycan and gene targets involved in glycan-mediated toxicity, for identifying helminths susceptible to glycan-mediated toxicity, and for identifying anti-helminthic and anti-allergic substances.

ANTI ALPHA-GALACTOSYL SCREENING TECHNIQUE

Compounds and libraries are labeled with a galactosyl epitope and then screened in accordance with an assay involving cells having a characteristic of interest. Conveniently, the screening may embody target cells, where the compounds are brought in contact with the cells. Each of the compounds carries with it the information of its identity or method of synthesis. After washing away non-specifically bound compounds, blood may be applied to the cells, whereby antibody binding to the galactosyl epitope initiates the complement cascade. Plaques are identified and the compound associated with the plaque identified. The formation of the plaque demonstrates that the compound has specific affinity for the target cell, binding of the compound to the cell does not interfere with binding of the antibody, and that the complex is capable of cytotoxic activity by means of the complement cascade.

MEANS AND METHODS FOR GLYCOPROFILING OF A PROTEIN

The present invention provides magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon including uses in methods for glycoprofiling of glycoproteins using lectins, e.g., in diagnostics of cancer. The magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein.

Новые моноклональные антитела к LAM и PIM6/LAM для диагностики и лечения инфекций, вызванных Mycobacterium tuberculosis

PROCEDURE FOR THE PRODUCTION OF VITAMIN K DEPENDENT PROTEINS

GLYKOLISIERTES INSULIN SUCH AS BIO MARKERS TO THE DIAGNOSIS AND MONITORING OF DIABETES

Method and composition for analyzing a carbohydrate polymer

Cancer specific oligosaccharide sequences and use thereof

Anti-CD27 antibody

Biomarkers for prostate cancer and methods for their detection

The invention provides a method for predicting the clinical response to a cancer vaccine in a patient having cancer, a method for determining the immune response to a cancer vaccine in a patient having cancer who has been administered a cancer vaccine, a method for determining the long-term survival in a patient having cancer, corresponding kits therefor, as well as methods of for improving the efficacy of a virus-based vaccine.

Antibodies, pharmaceutical compositions and uses thereof

The present invention provides antibodies or the antigen-binding portion thereof, that bind to one or more carbohydrate antigens. Also disclosed herein are pharmaceutical pharmaceutical compositions and methods for the inhibition of cancer cells in a subject in need thereof. The pharmaceutical compositions comprise an antibody or an antigen binding portion thereof and at least one pharmaceutically acceptable carrier.

Carbohydrate ligands that bind to IgM antibodies against myelin-associated glycoprotein

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM 5 antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (1) and (11) COONa HO COONa HO -S O1 0 OZ H - - 0 0 O NaO3SO OOZ HO Z OH OH (1) and OH OH (1|) 10 wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (1) and/or formula (11), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone.

Glycan analysis of proteins and cells

The present invention provides methods and compositions for glycan analysis of complex solutions, including proteins and cells in a biological sample. The method includes the preparation of substrates for the capture of proteins and cells for multiplexed analysis. Cells and proteins may be captured by antibody arrays, culture, or direct deposition. The invention further relates to the use of protein and cell glycan analysis in the diagnosis and screening of disease states and disease progression.

ANTI-GLYCATED CD59 ANTIBODIES AND USES THEREOF

The invention includes antibodies or antigen-binding fragments thereof which bind specifically to glycated CD59, compositions containing one or a combination of such antibodies or antigen-binding fragments thereof, hybridoma cell lines that produce the antibodies, and methods of producing and using the antibodies or antigen-binding fragments thereof for diagnosis and treatment of diabetic conditions and diabetic complications or diabetes-associated conditions. The invention also involves in some embodiments assays, diagnostics, kits, and assay components for determining levels of glycated CD59 in subjects. Treatments for subjects based upon levels of glycated CD59 also are provided.

STEROL GLUCOSIDE TOXINS

The invention relates to the identification of sterol glucoside toxins, and provides methods for detecting and detoxifying the compounds, as well as therapeutic methods for treating subjects exposed to such toxins. In alternative embodiments, the toxins may for example include beta-sitostrol-beta-D-glucoside (5-cholesten-24b-ethyl-3b-ol-D-glucoside) or cholesterol glucoside (5-cholesten-3b-ol-3b-D-glucoside).

POLYSACCHARIDE STRUCTURE AND SEQUENCE DETERMINATION

The invention provides a method for the structural analysis of a saccharide, comprising: a) providing on a surface a plurality of essentially sequence- and/or site-specific binding agents; b) contacting said surface with a saccharide to be analyzed, or with a mixture comprising a plurality of fragments of said saccharide; c) washing or otherwise removing unbound saccharide or saccharide fragments; d) adding to the surface obtained in step c) an essentially sequence- and/or site-specific marker, or a mixture of essentially sequence- and/or site-specific markers; e) acquiring one or more images of the markers that are bound to said surface; and f) deriving information related to the identity of the saccharide being analyzed from said image.

STEROL GLUCOSIDE TOXINS

In one aspect, the present invention discloses the neuronal excitotoxicicity of sterol glycosides. In alternative embodiments, sterol glycosides that are characterized by neuronal excitotoxicicity are .beta.-sitosterol-.beta.-D-glucoside (BSSG) and cholesterol glucoside.

OLIGOSIALIC ACID DERIVATIVES, METHODS OF MANUFACTURE, AND IMMUNOLOGICAL USES

Provided are methods of producing, and compositions comprising, isolated alpha (2?8) or (2?9) oligosialic acid derivatives bearing a non-reducing end enriched for one or more de-N-acetyl residues and resistant to degradation by exoneuraminidase. A representative production method involves: (i) treating an alpha (2?8) or (2?9) oligosialic acid precursor having a reducing end and a non-reducin end with sodium borohydride under conditions for de-N-acetylating the non-reducing end; and (ii) isolating alpha (2?8) or (2?9) oligosialic acid derivatives having one or more de-N-acetylated residues and a non-reducing end that is resistant to degradation by exoneuraminidase. Also provided are antibodies specific for the derivatives, kits, and methods of use including protection against and detection of E. coli K1 and N. meningitidis bacterial infection, and in diagnosing and treating cancer.

ANTI-CD27 ANTIBODY

The present invention provides a monoclonal antibody which specifically recognizes CD27 containing an O-linked sugar chain to which galactose is not bound and binds to its extracellular region, or a method for using the same. The present invention can provide a monoclonal antibody or an antibody fragment thereof, which specifically recognizes a polypeptide encoded by CD27 gene containing an O-linked sugar chain to which galactose is not bound, and binds to its extracellular region; a hybridoma which produces the antibody; a DNA which encodes the antibody; a vector which comprises the DNA; a transformant obtainable by transforming the vector; a process for producing an antibody or an antibody fragment thereof using the hybridoma or the transformant; and a diagnostic agent or a therapeutic agent comprising the antibody or the antibody fragment thereof as an active ingredient.

The combination of the anti-myelin-associated glycoprotein IgM antibody carbohydrate ligand

MARKER FOR DIABETIC COMPLICATIONS

The present invention addresses the problem of providing a marker with which diabetic complications can be examined. Provided is a marker for examining diabetic complications which comprises a compound represented by formula (1), or a salt thereof.

New monoclonal antibodies against pancreatic epitopes, useful for diagnosis and treatment of pancreatic disease, especially cancer, also new glycopeptide epitopes

Glycopeptide comprenant de 1 à 40 polypeptides répétés C-terminaux, composés de 11 acides aminés, de la BSDL ou de la FAPP, lesdits polypeptides étant glycosylés et portant des épitopes glycosylés donnant lieu à une réaction immunologique spécifique avec des anticorps induits chez un patient atteint par un diabète de type I et ou bien purifié à partir de fluides biologiques d'origine humaine ou animale ou bien recombinant et pouvant être produit par expression dans une cellule-hôte conventionnelle comprenant un matériel enzymatique nécessaire à l'amorçage d'une glycosylation, ladite cellule-hôte étant génétiquement modifiée de manière à comporter un gène codant pour lesdits polypeptides et un gène codant pour une ou plusieurs enzymes choisies parmi les glycosyltransférases, anticorps anti-glycopeptide et applications en thérapeutique et diagnostic.

METHOD FOR MEASUREMENT OF GLYCOPROTEIN, METHOD FOR DETECTION OF HEPATIC DISEASES, REAGENT FOR QUANTIFICATION OF GLYCOPROTEIN, AND SUGAR CHAIN MARKER GLYCOPROTEIN AS MEASURE OF DISEASE CONDITIONS OF HEPATIC DISEASES

Methods and reagents for the assessment of gestational diabetes

CARBOHYDRATE LIGANDS THAT BIND TO IGM ANTIBODIES AGAINST MYELIN-ASSOCIATED GLYCOPROTEIN

DIAGNOSIS OF CANCERS THROUGH GLYCOME ANALYSIS

Markers and methods of diagnosis and monitoring of cancer through global glycome analysis.

ADVANCED GLYCATION END-PRODUCT INTERMEDIARIES AND POST-AMADORI INHIBITION

The instant invention provides compositions and methods for modeling post-Amadori AGE formation and the identification and characterization of effective inhibitors of post-Amadori AGE formation, and such identified inhibitor compositions.

FACTOR VII GLYCOFORMS

The present invention relates to compositions comprising Factor VII and other blood clotting factors having altered patterns of asparagine-linked glycosylation.

METHOD FOR ANALYZING A GLYCOMOLECULE

The invention relates generally the structural analysis of glycomolecule-containing macromolecules, such as those that occur either attached to proteins (proteoglycans, glycoproteins), lipids, or as free saccharides.

METHOD FOR EVALUATION OF MULTIPLE ANTIBODIES OR MULTIPLE ANTIGENS IN A SINGLE SAMPLE

A multiplex assay for simultaneous detection of multiple antibodies or multiple antigens in single sample, wherein carboxylated polystyrene microsphere sets are conjugated with a defined candidate antigens by an optimized conjugation method and are mixed to enable the detection of multiple antibodies or multiple antigens, respectively. The multiplex assay of the invention is utilized for quantitation of antibody or antigen wherein minimum heterologous inhibition(cross-reactivity) of less than 20% for all serotypes and homologous inhibition greater than 80% can be obtained, wherein the polysaccharide coupled microspheres have been prepared by an optimal method without altering the critical epitopes of polysaccharide.

Assay for glycosylated proteins

The invention provides a method for assaying for a protein having at least two isoforms having different glycosylation patterns, said method comprising: contacting a sample containing said protein with a carbohydrate-binding agent and a ligand capable of binding to at least two said isoforms, and detecting conjugates of said carbohydrate-binding agent and said protein and/or of said ligand and said protein.

Methods, products and treatments for diabetes

The invention involves assays, diagnostics, kits, and assay components for determining levels of K41-glycated CD59 in subjects. Treatments for subjects based upon levels of K41-glycated CD59 also are provided.

Method of diagnosing breast cancer

By detecting the GalNAcβ1→4GlcNAcβ1→ structure expressed at the non-reducing termini of Asn-linked sugar chains of glycoproteins in samples prepared from cancer tissues or milk of patients with breast cancer, not only breast cancer but also the grades and malignancy levels of the breast cancers, prognosis of the breast cancer patients after surgery and etc. can be predicted accurately and effectively.

CLOSTRIDIUM PERFRINGENS SURFACE GLYCANS AND USES THEREOF

An immunogenic glycan compound has a poly-β-1,4-ManNAc repeating-unit structure variably modified with 6-linked phosphoethanolamine and 6-linked phosphoglycerol.

METHODS, PRODUCTS AND TREATMENTS FOR DIABETES

The invention involves assays, diagnostics, kits, and assay components for determining levels of K41-glycated CD59 in subjects. Treatments for subjects based upon levels of K41-glycated CD59 also are provided.

MANNOSE-6-PHOSPHATE-BINDING ANTIBODIES AND THEIR USES

C-erbB-2 EXTERNAL DOMAIN: GP75

PROBLEM TO BE SOLVED: To provide methods and compositions for identifying malignant tumors that overexpress c-erbB-2 oncogene. SOLUTION: This method is based on that an external domain glycoprotein (gp75) encoded by the c-erbB-2 oncogene or fragments thereof are detected in the biological fluids of mammals carrying a tumor burden. Detecting the external domain of c-erbB-2 and the glycoprotein gp75 and quantitating the level of gp75 in the biological fluids of mammals enable diagnosis and prognosis of neoplastic disease. COPYRIGHT: (C)2007,JPO&INPIT ...

Patent RU2016138744A3

РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2016 138 744 A (51) МПК A61K 39/00 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ЗАЯВКА НА ИЗОБРЕТЕНИЕ (21)(22) Заявка: 2016138744, 10.04.2015 (71) Заявитель(и): ОБИ ФАРМА ИНК. (TW) Приоритет(ы): (30) Конвенционный приоритет: 10.04.2014 US 61/977,824; 30.09.2014 US 62/057,381 (85) Дата начала рассмотрения заявки PCT на национальной фазе: 10.11.2016 US 2015/025305 (10.04.2015) (87) Публикация заявки PCT: A WO 2015/157629 (15.10.2015) Адрес для переписки: 119019, Москва, Гоголевский б-р, 11, этаж 3, "Гоулинг ВЛГ (Интернэшнл) Инк.", Карпенко Оксана Юрьевна R U (57) Формула изобретения 1. Антитело или его антигенсвязывающая часть, содержащие: первую определяющую комплементарность область тяжелой цепи (HCDR1), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 5 или SEQ ID NO: 31; вторую определяющую комплементарность область тяжелой цепи (HCDR2), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 6, SEQ ID NO: 24 или SEQ ID NO: 32; третью определяющую комплементарность область тяжелой цепи (HCDR3), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 7, SEQ ID NO: 25 или SEQ ID NO: 33; первую определяющую комплементарность область легкой цепи (LCDR1), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 8; вторую определяющую комплементарность область легкой цепи (LCDR2), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 9 или SEQ ID NO: 35; и Стр.: 1 A 2 0 1 6 1 3 8 7 4 4 (54) АНТИТЕЛА, ФАРМАЦЕВТИЧЕСКИЕ КОМПОЗИЦИИ И ИХ ПРИМЕНЕНИЯ 2 0 1 6 1 3 8 7 4 4 (86) Заявка PCT: R U (43) Дата публикации заявки: 11.05.2018 Бюл. № 14 (72) Автор(ы): ЛАЙ Цзянн-Шиюнь (TW), ЧЭНЬ И- ...

УГЛЕВОДНЫЕ ЛИГАНДЫ, КОТОРЫЕ СВЯЗЫВАЮТСЯ С IgM АНТИТЕЛАМИ ПРОТИВ МИЕЛИН-АССОЦИИРОВАННОГО ГЛИКОПРОТЕИНА

FIELD: medicine. SUBSTANCE: present invention relates to a compound of the formula (I-R) or formula (II-R), where R is phenyl, optionally substituted with a substituent selected from lower alkoxy, amino-lower alkyl or mercapto-lower alkankarbonylamino-lower alkyl, carbohydrate ligand that binds to IgM antibodies against myelin-associated glycoprotein (hereinafter – MAG), to polymer containing this ligand, and their use in the diagnostics and treatment of anti-MAG neuropathy. EFFECT: obtaining compounds for the treatment of anti-MAG neuropathy. (I-R), (II-R) 22 cl, 2 dwg, 1 tbl РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2 760 005 C2 (51) МПК C07H 15/203 (2006.01) A61K 31/7016 (2006.01) A61P 25/02 (2006.01) C08G 69/10 (2006.01) G01N 33/66 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ОПИСАНИЕ ИЗОБРЕТЕНИЯ К ПАТЕНТУ (52) СПК C07H 15/203 (2013.01); A61K 31/7016 (2013.01); A61P 25/02 (2013.01); C08G 69/10 (2013.01); G01N 33/06 (2013.01) (21)(22) Заявка: 2016134035, 12.03.2015 12.03.2015 Дата регистрации: 22.11.2021 13.03.2014 EP 14159528.0 (43) Дата публикации заявки: 13.04.2018 Бюл. № 11 (45) Опубликовано: 22.11.2021 Бюл. № 33 (86) Заявка PCT: EP 2015/055140 (12.03.2015) (87) Публикация заявки PCT: R U 2 7 6 0 0 0 5 WO 2015/136027 (17.09.2015) Адрес для переписки: 190900, Санкт-Петербург, BOX-1125, ПАТЕНТИКА (54) УГЛЕВОДНЫЕ ЛИГАНДЫ, КОТОРЫЕ СВЯЗЫВАЮТСЯ С IgM АНТИТЕЛАМИ ПРОТИВ МИЕЛИН-АССОЦИИРОВАННОГО ГЛИКОПРОТЕИНА (57) Реферат: Настоящее изобретение относится к нейропатии. 6 н. и 16 з.п. ф-лы, 2 ил., 1 табл. соединению формулы (I-R) или формулы (II-R), где R представляет собой фенил, необязательно (I-R), замещенный заместителем, выбранным из низшего алкокси, амино-низшего алкила или меркапто-низшего алканкарбониламино-низшего алкила, углеводному лиганду, который связывается с IgM антителами против миелин(II-R) ассоциированного гликопротеина (MAG), к полимеру, содержащему данный лиганд, и к их применению в диагностике и лечении анти-MAG Стр.: 1 C 2 C 2 ( ...

Patent RU2016134035A3

ВИ“? 2016134035” АЗ Дата публикации: 25.10.2018 Форма № 18 ИЗИМ-2011 Федеральная служба по интеллектуальной собственности Федеральное государственное бюджетное учреждение 5 «Федеральный институт промышленной собственности» (ФИПС) ОТЧЕТ О ПОИСКЕ 1. . ИДЕНТИФИКАЦИЯ ЗАЯВКИ Регистрационный номер Дата подачи 2016134035/04(052989) 12.03.2015 РСТ/ЕР2015/055140 12.03.2015 Приоритет установлен по дате: [ ] подачи заявки [ ] поступления дополнительных материалов от к ранее поданной заявке № [ ] приоритета по первоначальной заявке № из которой данная заявка выделена [ ] подачи первоначальной заявки № из которой данная заявка выделена [ ] подачи ранее поданной заявки № [Х] подачи первой(ых) заявки(ок) в государстве-участнике Парижской конвенции (31) Номер первой(ых) заявки(ок) (32) Дата подачи первой(ых) заявки(ок) (33) Код страны 1. 14159528.0 13.03.2014 ЕР Название изобретения (полезной модели): [Х] - как заявлено; [ ] - уточненное (см. Примечания) УГЛЕВОДНЫЕ ЛИГАНДЫ, КОТОРЫЕ СВЯЗЫВАЮТСЯ С М АНТИТЕЛАМИ ПРОТИВ МИЕЛИН-АССОЦИИРОВАННОГО ГЛИКОПРОТЕИНА Заявитель: УНИВЕРСИТЕТ БАЗЕЛЬ, СН 2. ЕДИНСТВО ИЗОБРЕТЕНИЯ [Х] соблюдено [ ] не соблюдено. Пояснения: см. Примечания 3. ФОРМУЛА ИЗОБРЕТЕНИЯ: [Х] приняты во внимание все пункты (см. Примечания) [ ] приняты во внимание следующие пункты: [ ] принята во внимание измененная формула изобретения (см. Примечания) 4. КЛАССИФИКАЦИЯ ОБЪЕКТА ИЗОБРЕТЕНИЯ (ПОЛЕЗНОЙ МОДЕЛИ) (Указываются индексы МПК и индикатор текущей версии) С07Н 15/203 (2006.01) Аб1К 31/7016 (2006.01) Аб1Р 25/02 (2006.01) С08С 69/10 (2006.01) СОМ 33/66 (2006.01) 5. ОБЛАСТЬ ПОИСКА 5.1 Проверенный минимум документации РСТ (указывается индексами МПК) СО7Н 15/203 Аб1К 31/7016 Аб1Р 25/02 С08С 69/10 001М№ 33/66 5.2 Другая проверенная документация в той мере, в какой она включена в поисковые подборки: 5.3 Электронные базы данных, использованные при поиске (название базы, и если, возможно, поисковые термины): РЕРАТБ пе, ЕАРАТТУ, Езрасепе, боозе, РАТЕМТСОРЕ, Рабеагсв, КОРТО, ЗГРО, (см. на ...

УГЛЕВОДНЫЕ ЛИГАНДЫ, КОТОРЫЕ СВЯЗЫВАЮТСЯ С IgM АНТИТЕЛАМИ ПРОТИВ МИЕЛИН-АССОЦИИРОВАННОГО ГЛИКОПРОТЕИНА

VERFAHREN ZUR HERSTELLUNG VITAMIN-K-ABHÄNGIGER PROTEINE

STRUKTUR- UND SEQUENZBESTIMMUNG VON POLYSACCHARIDEN

THE INTERMEDIAIRES PRODUITS DEFINITIFS DE GLYCOSYLATION AVANCEE ET INHIBITION OF THE PRODUITS AGE POST OFFICE AMADORI

GLYKOFORMEN FROM FACTOR VII

PROCEDURE AND COMPOSITIONS FOR THE MEASUREMENT OF NATRIURETI PEPTIDEN AND USE FOR IT

PROCEDURE FOR THE INVESTIGATION OF KOLONKARZINOM AND KOLONADENOM

ASSAY FOR GLYCOSYLATED PROTEINS

CAMPYLOBACTER GLYCANS AND GLYCOPEPTIDES

Carbohydrate-containing pan cancer marker

Carbohydrate ligands that bind to IgM antibodies against myelin-associated glycoprotein

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone.

Anti-MUC1 antibody or antigen-binding fragment of same, and use thereof

The present invention provides: an antibody exhibiting specificity for MUC1, the antibody having a glycan structure expressed at high levels in cancer cells; a method for manufacturing this antibody; and a novel means and method for the diagnosis and prevention and/or treatment of cancer using this antibody. The present invention is a monoclonal antibody to human MUC1, wherein the antibody specifically recognizes a glycopeptide having a human MUC1 tandem unit and furthermore having an O-linked glycan core (0(Tn)) in any one of the threonine and serine in the amino acid sequence of this human MUC1 tandem unit. A method for detecting MUC1 in a human body-fluid sample. A kit including this monoclonal antibody. A pharmacological composition for the prevention and/or treatment of a malignant tumor, the pharmacological composition containing this monoclonal antibody as an active ingredient.

METHOD FOR CLEAVING AND DEGLYCOSYLATING ANTIBODIES TO PROMOTE LIGAND BINDING

The present invention details methods to detect glycoproteins in samples to identify a disease state. In particular, an improved sandwich assay is described, using both an antibody and an array of lectins. Methods for increasing the efficiency of interaction of an antibody with a ligand by cleaving the antibody to remove the carbohydrate moiety, and orienting the cleaved fragment on a matrix to enhance recognition of a ligand are also described. Methods of differentiating pregnancy-derived and disease derived samples are also described.

A MARKER FOR MEASURING LIVER CIRRHOSIS

The invention provides methods and kits to detect liver cirrhosis in mammals. The diagnostic test is based on the profiling and identification of diagnostic carbohydrates present in a body fluid such as blood serum.

ANTIBODY-DRUG CONJUGATES CONTAINING ANTI-GLOBO H ANTIBODIES AND USES THEREOF

An immunoconjugate includes an anti-Globo H antibody, or a binding fragment thereof, and a therapeutic agent or a label, having the formula: Ab-(L-D)m, wherein Ab is the anti-Globo H antibody or the binding fragment thereof, L is a linker or a direct bond, D is the therapeutic agent or the label, and m is an integer from 1 to 8. The antibody may be a monoclonal antibody, which may be a humanized antibody. A method for treating a cancer includes administering to a subject in need of such treatment a pharmaceutically effective amount of an immunoconjugate containing an antibody against Globo H, or a binding fragment thereof, and a therapeutic agent covalently conjugated with the antibody.

MEANS AND METHODS FOR GLYCOPROFILING OF A PROTEIN

The present invention provides magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon including uses in methods for glycoprofiling of glycoproteins using lectins, e.g., in diagnostics of cancer. The magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein.

METHODS AND REAGENTS FOR THE ASSESSMENT OF GESTATIONAL DIABETES

The invention involves assays, diagnostics, kits, and assay components for determining levels of glycated CD59 in the assessment of gestational diabetes mellitus and/or related disorders and/or conditions. Some kits comprise a capture antibody capable of associating with a capture epitope on CD59, wherein said capture epitope may lack lysine residue number 41 (K41 ). Kits may also comprise a detection antibody capable of associating with a detection epitope on CD59. Such detection epitopes may comprise glycated K41.

ANTI ALPHA-GALACTOSYL SCREENING TECHNIQUE

Compounds and libraries are labeled with a galactosyl epitope and then screened in accordance with an assay involving cells having a characteristic of interest. Conveniently, the screening may embody target cells, where the compounds are brought in contact with the cells. Each of the compounds carries with it the information of its identity or method of synthesis. After washing away non-specifically bound compounds, blood may be applied to the cells, whereby antibody binding to the galactosyl epitope initiates the complement cascade. Plaques are identified and the compound associated with the plaque identified. The formation of the plaque demonstrates that the compound has specific affinity for the target cell, binding of the compound to the cell does not interfere with binding of the antibody, and that the complex is capable of cytotoxic activity by means of the complement cascade.

ADVANCED GLYCATION END-PRODUCT INTERMEDIARIES AND POST-AMADORI INHIBITION

The instant invention provides compositions and methods for modeling postAmadori AGE formation and the identification and characterization of effective inhibitors of post-Amadori AGE formation, and such identified inhibitor compositions.

GLYCOPEPTIDES DERIVED FROM PANCREATIC STRUCTURES, ANTIBODY AND THEIR APPLICATIONS IN DIAGNOSIS AND THERAPEUTIC

PROCESS OF DETERMINATION Of the GLYCOSYLATION Of an ANTIBODY

Non-invasive brain injury diagnostic device

AN ANALYZING METHOD FOR MEASURING THE CHANGES OF GLYCOSYLATION IN VARIOUS GLYCOPROTEIN

The present invention relates to an analyzing method of measuring the changes of glycosylation in various glycoproteins which participate in carcinogenesis and metastasis.

Anti-CD27 antibody

The present invention provides a monoclonal antibody which specifically recognizes CD27 containing an O-linked sugar chain to which galactose is not bound and binds to its extracellular region, or a method for using the same. The present invention can provide a monoclonal antibody or an antibody fragment thereof, which specifically recognizes a polypeptide encoded by CD27 gene containing an O-linked sugar chain to which galactose is not bound, and binds to its extracellular region; a hybridoma which produces the antibody; a DNA which encodes the antibody; a vector which comprises the DNA; a transformant obtainable by transforming the vector; a process for producing an antibody or an antibody fragment thereof using the hybridoma or the transformant; and a diagnostic agent or a therapeutic agent comprising the antibody or the antibody fragment thereof as an active ingredient.

GLYCOPEPTIDE AND USES THEREOF

A glycolipopeptide comprising a carbohydrate component, a peptide component and a lipid component, for use as a therapeutic or prophylactic vaccine. Also provided are monoclonal and polyclonal antibodies that recognize the glycolipopeptide of the invention, as well as uses thereof.

Biomarkers for assessment of preeclampsia

Disclosed herein are screening tools for fetal/maternal wellness, such as biomarkers for assessing preeclampsia. More specifically, methods are disclosed for assessing the risk of preeclampsia in a subject, the methods including obtaining a first serum sample from the subject, determining a level of glycosylated fibronectin (GlyFn) in the first serum sample, and comparing the determined level of GlyFn with a control value, wherein an elevation in the determined level of GlyFn in the first serum sample relative to the control value indicates that the subject is at increased risk of preeclampsia. Also disclosed are methods of determining the risk of preeclampsia in a subject during a first, second, or third trimester, methods of assessing severity and progression of preeclampsia and complications of a risk of low birth weight or HELLP syndrome.

Element, method and kit for the determination of an analyte in a fluid

The present invention relates to a method for detection of carcinoembryonic antigens (hereinafter abbreviated as CEAs) having a modified sugar chain structure which comprises using an antibody against a constant region of CEAs and a protein capable of recognizing a modified sugar chain structure of CEAs, a method for detecting a cancer which comprises using an amount of CEAs having a modified sugar chain structure and a kit for detection of CEAs having a modified sugar chain structure which comprises an antibody against a constant region of CEAs and a protein capable of recognizing a modified sugar chain structure of CEAs. Said method and kit are useful in a separately measurement of the various CEAs, a detection of a cancer and a definition of the kind of a cancer, and, for example, by using in proper combination of the measurement value of various CEAs obtained by the method of the present invention, it becomes possible to detect the cancer or define the kind of the cancer.

ADVANCED GLYCATION END-PRODUCT INTERMEDIARIES AND POST-AMADORI INHIBITION

IMMUNOCHROMATOGRAPHIC DEVICE FOR EXTRACTING AND MEASURING CARBOHYDRATE ANTIGENS

Galactose-Alpha-1,3-Galactose-Macromolecule Conjugates And Methods Employing Same

Methods and reagents are disclosed for conducting assays for IgE. Embodiments of the present reagents comprise a conjugate of a macromolecule and a compound comprising a galactose-α-1,3-galactose epitope. Embodiments of the present methods are directed to determining the presence and/or amount of an IgE specific for a galactose-α-1,3-galactose epitope in a sample. A combination is provided in a medium, which comprises the sample and a reagent for determining the presence and/or amount of an IgE specific for a galactose-α-1,3-galactose epitope in a sample wherein the reagent comprises a conjugate of a macromolecule and a compound comprising a galactose-α-1,3-galactose epitope. The combination is subjected to conditions for binding of the IgE to the reagent to form a complex. The presence and/or amount of the complex are detected and the amount of the complex is related to the presence and/or amount of IgE in the sample.

Brassica gat event and compositions and methods for the identification and/or detection thereof

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

BREAST-CANCER DETERMINATION METHOD

The present invention provides a breast cancer marker selected from the group consisting of fucosylated hornerin, fucosylated Zn-α-2-glycoprotein, fucosylated Ig γ-1 chain C region, and fucosylated desmoplakin; a method for determining breast cancer comprising detecting the breast cancer marker in a sample, and determining on the basis of the results of the results; and a kit to be used for the determination. 1. A breast cancer marker selected from the group consisting of fucosylated hornerin , fucosylated Zn-α-2-glycoprotein , fucosylated Ig γ-1 chain C region , and fucosylated desmoplakin.2. A method for obtaining a data for determining breast cancer , comprising detecting one or more breast cancer markers selected from the group consisting of fucosylated hornerin , fucosylated Zn-α-2-glycoprotein , fucosylated Ig γ-1 chain C region , and fucosylated desmoplakin in a sample.3. The method according to claim 2 , wherein the sample is nipple discharge.4. The method according to claim 2 , wherein the sample is serum claim 2 , plasma claim 2 , or whole blood.5. A method for determining breast cancer claim 2 , comprising:detecting one or more breast cancer markers selected from the group consisting of fucosylated hornerin, fucosylated Zn-α-2-glycoprotein, fucosylated Ig γ-1 chain C region, and fucosylated desmoplakin in a sample, anddetermining on the basis of the results thereof.6. The method according to claim 5 , wherein the sample is nipple discharge.7. The method according to claim 5 , wherein the sample is serum claim 5 , plasma claim 5 , or whole blood.8. A kit for detecting a breast cancer marker for determining breast cancer comprising a reagent for detecting a breast cancer marker selected from the group consisting of fucosylated hornerin claim 5 , fucosylated Zn-α-2-glycoprotein claim 5 , fucosylated Ig γ-1 chain C region claim 5 , and fucosylated desmoplakin.9. The kit according to claim 8 , wherein the reagents for detecting a breast cancer marker comprises ...

THE DETECTION OF FREE AND PROTEIN-BOUND NON-HUMAN GAL-ALPHA(1-3)-GAL EPITOPE

The present invention relates to the provision of antibody fragments capable of binding selectively to the Gal-α-(1→3)-Gal epitope. The invention further relates to assay systems comprising these antibody fragments for use in testing transplantation tissue for possible rejection complications. This epitope is often found on porcine tissue destined for human transplantation. The epitope is also found on biopharmaceuticals and on some infectious agents and accordingly the invention also provides assay systems for these applications. 2. An antibody as claimed in comprising all of the sequences (1) to (3) or (5) to (7) or sequences with at least 80% homology with any of those sequences.4. An antibody as claimed in or wherein the antibody is a monoclonal antibody claim 1 , an scFv fragment or an Fab fragment.5. An antibody as claimed in which is selected from fragments having the sequence IDs. Nos 2 claim 1 , 3 or 4.6. An scFv antibody fragment as claimed in which is Sequence ID No. 2.7. An assay kit for the determination of the presence or the quantification of a Gal-α-(1→3)-Gal motif in tissues or cells or on proteins claim 1 , comprising at least one antibody as claimed in or .8. An assay as claimed in further comprising the reagents and/or instructions for an ELISA assay claim 7 , a competitive/inhibition ELISA claim 7 , a sandwich ELISA assay claim 7 , a micro-array based assay claim 7 , a functionalised nanoparticle assay claim 7 , other rapid assay platform such as quantum dots claim 7 , fluorescent tags and electrosensors claim 7 , an immunohistochemistry assay claim 7 , or a flow cytometry assay.9. A method of determining the presence of claim 1 , or of quantifying the amount of a Gal-α-(1→3)-Gal motif in tissues or cells or on proteins claim 1 , comprising determining the degree of binding of an antibody or fragment as claimed in to the tissue claim 1 , cell or protein.10. A pharmaceutical composition comprising an antibody fragment as claimed in together with ...

NON-INVASIVE BRAIN INJURY DIAGNOSTIC DEVICE

Disclosed is a device for conducting a non-invasive diagnostic test in a subject suspected of suffering brain injury. The device for diagnosing a brain injury in a subject includes a probe of a porous matrix, an indicator formulation disposed on the porous matrix and includes at least one lectin and/or antibody capable of selectively binding to a glycan-based biomarker indicative of brain injury in a sample, and a visually detectable label; and a handle in communication with the probe, wherein at least one of the lectin and/or antibody and/or the visually detectable label is immobilized in and/or on a detection zone in the porous matrix, and the visually detectable label develops a color intensity level and becomes visible upon a binding event of the glycan-based biomarker to the lectin and/or antibody. Also provided is a method for using the device described below and methods for producing the same. 124-. (canceled)25. A device for diagnosing a brain injury in a subject , comprising:a probe, said probe comprises a porous matrix; andan indicator formulation disposed in and/or on said porous matrix and comprises at least one glycan-based biomarker binding reagent for selectively binding to a glycan-based biomarker in a sample, and a first visually detectable label;wherein:at least one of said glycan-based biomarker binding reagent and/or said first visually detectable label is immobilized in and/or on a detection zone in said porous matrix;said glycan-based biomarker is indicative of brain injury;said first visually detectable label develops a color and becomes visible upon a binding event of said glycan-based biomarker to said glycan-based biomarker binding reagent; andsaid binding event is effected by contacting said sample with said probe.26. The device of claim 25 , wherein said glycan-based biomarker binding reagent is a lectin and/or an antibody.27. The device of claim 25 , wherein said first visually detectable label is attached to said glycan-based biomarker ...

GLYCOPEPTIDE AND USES THEREOF

A glycolipopeptide comprising a carbohydrate component, a peptide component and a lipid component, for use as a therapeutic or prophylactic vaccine. Also provided are monoclonal and polyclonal antibodies that recognize the glycolipopeptide of the invention, as well as uses thereof. 1. A method for making an antibody comprising: at least one carbohydrate component comprising a B-epitope;', 'at least one peptide component comprising a T-epitope; and', 'at least one lipid component;', 'wherein the carbohydrate component comprises a saccharide selected from the group consisting of N-acetylglucosamine (GlcNAc), N-acetylgalactosamine (GalNAc), mannose, fucose and glucose; and, 'injecting into a mammal a glycolipopeptide comprisingisolating from the mammal at least one antibody that binds to the glycolipopeptide.221.-. (canceled)22. An antibody made according to the method of .23. A method for making an antibody comprising: at least one carbohydrate component comprising a B-epitope;', 'at least one peptide component comprising a T-epitope; and', 'at least one lipid component;', 'wherein the carbohydrate component comprises a saccharide selected from the group consisting of N-acetylglucosamine (GlcNAc), N-acetylgalactosamine (Ga1NAc), mannose, fucose and glucose;, 'injecting into a mammal a glycolipopeptide comprisingharvesting cells from the mammal;fusing the cells with myeloma cells to form hybridomas;selecting at least one hybridoma producing an antibody which binds to the glycolipopeptide; andisolating the antibody.24. The method of wherein the cells are spleen cells or lymph cells.25. The method of claim 23 , wherein the carbohydrate component comprises a self-antigen comprising the B-epitope.26. The method of claim 25 , wherein the self-antigen comprises a MUC-1 glycopeptide.27. The method of claim 23 , wherein the lipid component comprises PamCysSK claim 23 , wherein n=0 claim 23 , 1 claim 23 , 2 claim 23 , 3 claim 23 , 4 claim 23 , or 5.28. The method of claim 23 , ...

CARBOHYDRATE LIGANDS THAT BIND TO IGM ANTIBODIES AGAINST MYELIN-ASSOCIATED GLYCOPROTEIN

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone. 2. The compound of of formula (I) or (II) wherein Z is unsubstituted or substituted phenyl.3. The compound of of formula (I) or (II) wherein Z is p-methoxyphenyl.4. The compound of of formula (I) wherein Z is p-methoxyphenyl.5. The compound of of formula (II) wherein Z is p-methoxyphenyl.7. The polymer according to wherein the polymer backbone is an α-amino acid polymer claim 6 , an acrylic acid or methacrylic acid polymer or copolymer claim 6 , or a N-yinyl-2-pyrrolidone-yinyl alcohol copolymer.8. The polymer according to wherein the polymer backbone is an α-amino acid polymer claim 6 , wherein the α-amino acid is lysine claim 6 , glutamic acid or aspartic acid.9. The polymer according to wherein the polymer backbone is poly-lysine.10. The polymer according to wherein the molecular weight of the polymer backbone is 1′000 kD to 300′000 kD.11. The polymer according to any one of to claim 7 , wherein the linker Z is aryl claim 7 , heteroaryl claim 7 , aryl-lower alkyl claim 7 , arylcarbonyl claim 7 , or heteroarylmethyl claim 7 , wherein aryl or heteroaryl is substituted by alkylene with 3 to 25 carbon atoms connecting to the polymer wherein optionally(a) one or more carbon atoms of alkylene are replaced by nitrogen carrying a hydrogen atom, and one of the adjacent carbon atoms is substituted by oxo, representing an amide function —NH—CO—; and/ ...

METHOD FOR DETERMINING THE GLYCOSYLATION OF AN ANTIBODY

The invention relates to a method for detecting the binding of an antibody to an Fc receptor present on the surface of a cell as well as to a method for determining the level of glycosylation of an antibody. The invention also relates to a reagent kit for carrying out these methods. 1. An in vitro method for determining the binding of an antibody to an Fc receptor expressed in cell membranes or intact cells present in a measurement medium , comprising the following steps:(i) direct or indirect labeling of said Fc receptor with the first member of a pair of FRET partners, or else introducing, into the medium, cell membranes or intact cells whose Fc receptors were labeled beforehand directly with the first member of a pair of FRET partners;(ii) adding said antibody, labeled directly or indirectly with the second member of said pair of FRET partners, to the measurement medium;(iii) measuring the FRET signal, the existence of a FRET signal being representative of the binding of the antibody to the Fc receptor.2. The method as claimed in claim 1 , which is repeated with different antibody concentrations and which comprises an additional step (iv) of determining the dissociation constant of the antibody-Fc receptor bond.3. An in vitro method for determining the binding of a competing antibody with an Fc receptor expressed in cell membranes or intact cells present in a measurement medium claim 1 , by competition with a reference antibody claim 1 , comprising the following steps:(i) direct or indirect labeled of said Fc receptor with the first member of a pair of FRET partners, or else introducing, into the medium, cell membranes or intact cells whose Fc receptors were labeled beforehand directly with the first member of a pair of FRET partners;(ii) adding the competing antibody to the measurement medium;(iii) adding a reference antibody, labeled directly or indirectly with the second member of said pair of FRET partners, to the measurement medium;(iv) measuring the FRET ...

NOVEL ANTI-LAM AND ANTI-PIM6/LAM MONOCLONAL ANTIBODIES FOR DIAGNOSIS AND TREATMENT OF MYCOBACTERIUM TUBERCULOSIS INFECTIONS

The present invention broadly provides different compositions, kits, vectors, and methods including monoclonal antibodies directed to epitopes found within lipoarabinomannan (LAM) and phosphatidyl-myo-inositol mannoside 6 (PIM6) for the diagnosis and treatment of infections. 1. A human monoclonal anti-lipoarabinomannan (anti-LAM) antibody , or an antigen-binding portion thereof , that specifically binds to a LAM epitope comprising an Ara4 structure , an Ara6 structure , or a combination thereof , wherein the anti-LAM antibody comprises a CDR1 variable light region having at least 80% identity with SEQ ID NO: 1 or antigenic fragments thereof , a CDR2 variable light region having at least 80% identity with SEQ ID NO: 2 or antigenic fragments thereof , a CDR3 variable light region having at least 80% identity with SEQ ID NO: 3 or SEQ ID NO: 26 or antigenic fragments thereof , a CDR1 variable heavy region having at least 80% identity with SEQ ID NO: 4 or antigenic fragments thereof , a CDR2 variable heavy region having at least 80% identity with SEQ ID NO: 5 or antigenic fragments thereof , and a CDR3 variable heavy region having at least 80% identity with SEQ ID NO: 6 or SEQ ID NO: 23 or antigenic fragments thereof.2. The human monoclonal anti-LAM antibody or antigen-binding portion thereof of claim 1 , said antibody comprising a heavy chain variable region comprising the amino acid sequences of SEQ ID NO:21 and SEQ ID NO:23 claim 1 , and a light chain variable region comprising the amino acid sequences of SEQ ID NO: 24 and SEQ ID NO:26.3. The human monoclonal anti-LAM antibody or antigen-binding portion thereof of claim 1 , wherein the anti-LAM antibody is an scFv-IgG claim 1 , and IgGa or an IgM antibody.4. A human monoclonal anti-LAM antibody or an antigen-binding portion thereof claim 1 , that specifically binds to a LAM epitope comprising at least one of: a mannose-capped Ara4 structure and a mannose-capped Ara6 structure.5. The human monoclonal anti-LAM antibody ...

MEANS AND METHODS FOR GLYCOPROFILING OF A PROTEIN

The present invention provides magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon including uses in methods for glycoprofiling of glycoproteins using lectins, e.g., in diagnostics of cancer. The magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein. 1. A method of determining the glycoprofile of a protein , comprising(a) contacting a sample comprising said protein with an antibody directed against said protein to form an antibody-protein complex;(b) isolating the antibody-protein complex obtained in step (a); and(c) contacting the antibody-protein complex with one or more lectins to determine the glycoprofile of said protein,wherein wherein said antibody of step (a) is not immobilized on a solid surface, and wherein said protein is not released from said antibody while performing the method.2. The method of any one of the preceding claims , further comprising step (d) comparing the glycoprofile of said protein with a control glycoprofile of said protein to determine whether the glycoprofile of said protein may deviate from the glycoprofile of said control glycoprofile.3. The method of any one of the preceding claims , wherein said protein is a cancer biomarker protein , an autoimmune disease biomarker protein or an inflammatory disease biomarker protein.4. The method of claim 3 , wherein said cancer biomarker protein is an ovarian cancer biomarker protein claim 3 , breast cancer biomarker protein claim 3 , colorectal cancer biomarker protein claim 3 , pancreatic cancer biomarker protein claim 3 , prostate cancer biomarker protein claim 3 , thyroid cancer biomarker protein claim 3 , liver cancer biomarker protein claim 3 , lung cancer biomarker protein claim 3 , stomach cancer biomarker protein claim 3 , testicular cancer ...

Immunochromatographic test piece for extracting and measuring sugar chain antigen, which is capable of preventing non-specific reaction

It is intended to provide an immunochromatographic test piece which prevents a non-specific reaction by efficiently and continuously contacting and neutralizing a developing solution containing nitrous acid with a neutralizing reagent in an immunochromatography method of extracting and measuring a sugar chain antigen by nitrous acid extraction on the immunochromatographic test piece. The present invention provides an immunochromatographic test piece for extracting and measuring a sugar chain antigen in a specimen, the immunochromatographic test piece comprising: a sample pad to which a specimen mixed with nitrite or an acid solution is added; a label region comprising a labeled antibody obtained by labeling an antibody against the sugar chain antigen; and a detection region on which the antibody against the sugar chain antigen is immobilized, wherein an antibody-sugar chain antigen-labeled antibody complex is formed in the detection region to measure the sugar chain antigen, and the immunochromatographic test piece having a region impregnated with a neutralizing reagent upstream of the label region, and further having a region impregnated with a solid acid reagent when the specimen mixed with the nitrite is used, or a region impregnated with nitrite when the specimen mixed with the acid solution is used, upstream of the region impregnated with the neutralizing reagent, wherein a material for the region impregnated with the neutralizing reagent is a filter or a glass filter having three properties of being highly absorbable, being highly water-retainable, and being low releasable or continuously releasable, and owing to the high water-absorbable property and the high water-retainable property of the region impregnated with the neutralizing reagent, the acid solution containing the sugar chain antigen is sufficiently neutralized, and owing to the low releasable property or the sustained releasable property of the region impregnated with the neutralizing reagent, a ...

BIOMARKERS FOR PROSTATE CANCER AND METHODS FOR THEIR DETECTION

The invention provides a method for predicting the clinical response to a cancer vaccine in a patient having cancer, a method for determining the immune response to a cancer vaccine in a patient having cancer who has been administered a cancer vaccine, a method for determining the long-term survival in a patient having cancer, corresponding kits therefor, as well as methods of for improving the efficacy of a virus-based vaccine. 142.-. (canceled)43. A method for predicting the clinical response to a poxvirus-based vaccine in a patient and treating cancer in the patient , the method comprising:obtaining a serum sample from a patient having cancer who has not been previously administered the poxvirus-based vaccine;{'sub': di', 'di', 'di, 'assaying the serum sample to determine the levels of antibodies in the patient to at least one glycan and/or glycoprotein antigen selected from the group consisting of Sialylα2-6Galβ1-4Glc-(6′SLac), Sialylα2-3Galβ1-4(Fucα1-3)GlcNAc-(SLeX), Sialylα2-3Galβ1-4Glc-(GM3), Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4Glcβ-(BG-H1), GalNAcβ1-4Galβ-(GA2), Galβ1-4GlcNAcβ1-6(Galβ1-4GlcNAcβ1-3)Galβ-(LNnH), Galα1-3Gal-(B), Ac-Ser-(GalNAcα)Thr-Gly-Gly-(Ac-S-Tn(Thr)-G-G), BSM, Lactose, Galβ1-3GlcNAcβ1-3Galβ-(LNT), Fuc-b, Fuc-a, Galβ1-6Man-α-(Galb1-6Man-a), Galβ1-3GalNAcβ1-4Galβ1-(GA1), Galα1-4Galβ-(Gala1-4Galb), Manα1-6[Manα1-3]Manβ-(ManT), Galβ1-3GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-(pLNH), Rha-a-, GalNAcα1-3Galβ-(A), GalNAcα1-3(Fucα1-2)Galβ-(BG-A), Galβ1-3GalNAcβ1-4Galβ1-(GA1), fetuin, and Ac-Ser-(GalNAcα)Ser-Ser-Gly-(Ac-S-Tn(Ser)-S-G);'}comparing the determined levels of antibodies to the at least one glycan and/or glycoprotein antigen to a control, so as to predict the clinical response to the poxvirus-based vaccine in the patient; andtreating the cancer by administering the poxvirus-based vaccine to the patient.44. The method of claim 43 , wherein the serum sample is assayed to determine the levels of antibodies to at least two glycan and/or glycoprotein ...

ASSAYS FOR B-TYPE NATRIURETIC PEPTIDE ANALOGUES RESISTANT TO PROLYL-SPECIFIC DIPEPTIDYL DEGRADATION

The present invention describes compositions and methods for treating cardiovascular disease and myocardial infarction using dipeptidyl peptidase inhibitors. Also provided are methods for increasing natriuretic peptide function by administering one or more analogues of B type natriuretic peptide that provide increased stability in the presence of prolyl-specific dipeptidyl peptidases. 1. A method for the treatment of cardiovascular disease comprisinga) contacting a sample from a subject with a first antibody selected to bind biologically active forms of the natriuretic peptide of interest contacting the sample with a second antibody selected to bind all biologically active and biologically inactive forms of the natriuretic peptide of interest and performing an assay in which the signal depends upon the selected antibody specifically binding to a biologically active form of the natriuretic peptide of interest, but not specifically binding to a biologically inactive form of the natriuretic peptide of interest; andb) administering a therapeutically effective amount of a dipeptidyl peptidase inhibitor to said subject when the presence of said biologically active form of said natriuretic peptide is present, and wherein said administration preserves the presence of said biologically active form of said natriuretic peptide.217.-. (canceled)18. The method of claim 1 , wherein said biologically active natriuretic peptide of interest is BNP-32.19. The method of claim 1 , wherein the first and/or second antibodies are each conjugated to a detectable label.20. The method of claim 19 , wherein the label is a fluorescent or luminescent tag claim 19 , a metal claim 19 , a dye claim 19 , a radionuclide claim 19 , or an enzyme.21. The method of claim 1 , wherein the first and/or second antibodies are immobilized onto a solid support.22. The method of claim 21 , wherein the solid support is a magnetic particle claim 21 , a chromatographic matrix particle claim 21 , the surface of an ...

CARBOHYDRATE LIGANDS THAT BIND TO IGM ANTIBODIES AGAINST MYELIN-ASSOCIATED GLYCOPROTEIN

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone. 116.-. (canceled)19. The method of claim 18 , further comprising contacting polylysine with chloroacetic anhydride to prepare the chloroacetylated polylysine polymer.24. The method of claim 17 , wherein 30% to 60% of the lysine sidechains in the polylysine polymer are linked to the disaccharide substituents of formula (I) or a salt thereof.25. The method of claim 17 , wherein the method further comprises isolating and purifying the HNK-1 polymer.29. The method of claim 27 , wherein the contacting step is performed in DMF solvent in the presence of triethylamine. The invention relates to carbohydrate ligands that bind to IgM antibodies against myelin-associated glycoprotein (MAG), polymers comprising these, and to their use in diagnosis and therapy of anti-MAG neuropathy.Anti-myelin-associated glycoprotein neuropathy is a demyelinating peripheral neuropathy, caused by autoantibodies recognizing the antigenic HNK-1 carbohydrate epitope, found on myelin-associated glycoprotein (MAG) and other glycoconjugates of the peripheral nervous system (PNS). The clinical picture is characterized by a slowly progressing demyelinating, predominantly sensory neuropathy. The correlation of high levels of antibodies and demyelination is well established. Thus, pathological studies on nerve biopsies from patients show demyelination and widening of myelin lamellae ...

MELANOTRANSFERRIN FOR USE IN THE DIAGNOSIS OF PARKINSON`S DISEASE

The present invention is the protein of melanotransferrin, or an encoding nucleic acid of same, for use in the diagnosis of Parkinson's disease (PD). The invention is a method of diagnosis of PD in a subject, for assessing the level of melanotransferrin in the saliva or in a saliva sample of the subject and determining whether the level is above or below a value of 8.6 μg/ml, wherein a value below 8.6 μg/ml is indicative of PD. Another aspect is a kit having at least one reagent, preferably an antibody, for the quantification of melanotransferrin in the saliva or in a saliva sample of a subject enabling the comparison of the quantification with a predetermined cut-off value. 1. A method of diagnosis of Parkinson's disease using melanotransferrin in the saliva or in a saliva sample of a subject.2. A method of diagnosis of Parkinson's disease in a subject showing phenoconversion of a neurological disease , said method comprising:assessing the level of melanotransferrin in the saliva or in a saliva sample of said subject, anddetermining whether said level is above or below a value of 8.6 μg/ml, whereina value below 8.6 μg/ml is indicative of Parkinson's disease.3. Method according to claim 2 , in which said level value is 4 μg/ml.4. Method according to claim 2 , in which said subject is a mammal.5. A method according to claim 4 , in which said mammal is human. The present invention is of application in the medical science, in particular in the diagnosis of the Parkinson's disease.Parkinson's Disease (PD) is an age-related neurodegenerative disorder of unknown origin of high prevalence and consequent social and economic burden. The disease is involved with a multisystem neurodegenerative disorder that afflicts nearly 1% of people above the age of 60.PD neuropathology deals with a selective loss of dopaminergic neurons in the “substantia nigra pars compacta” (SNpc). A widespread involvement of other Central Nervous System (CNS) structures and peripheral tissues is widely ...

Methods and compositions for treating and diagnosing autoimmune diseases

The application relates to methods for the diagnosis, treatment, and prevention of autoimmune and/or inflammatory disease such as systemic lupus erythematosus (SLE), lupus nephritis, IgA nephropathy, other types of glomerulonephritis.

METHODS FOR DETERMINING PRESENCE OR ABSENCE OF GLYCAN EPITOPES ON GLYCOPROTEINS

The disclosure relates to in vitro methods of detecting presence or absence of a target carbohydrate on a glycoprotein. The disclosure also relates to in vitro methods of detecting presence or absence of a glycan epitope on a glycoprotein. 1. An in vitro method of determining presence or absence of a target carbohydrate on a target glycoprotein , comprising:providing a sample containing a target glycoprotein;treating the sample with a glycosidase, wherein the glycosidase removes a target carbohydrate if present on the target glycoprotein, thereby creating a vacant glycosylation acceptor site;treating the sample with a glycosyltransferase to incorporate a replacement carbohydrate into the vacant glycosylation acceptor site if present, wherein the replacement carbohydrate includes a click chemistry moiety;adding a label to the sample, wherein the label includes a click chemistry moiety that reacts to the click chemistry moiety of the replacement carbohydrate such that that the label attaches to the replacement carbohydrate;separating the sample using a separation method;determining presence or absence of label attached to the replacement carbohydrate in the separated sample; andcorrelating presence of the label to presence of the target carbohydrate or correlating absence of the label to absence of the target carbohydrate.2. The method of further comprising correlating presence of the target carbohydrate to presence of a glycan epitope or correlating absence of the target carbohydrate to absence of the glycan epitope.3. The method of wherein the separation method is an electrophoresis method.4. The method of wherein the replacement carbohydrate includes a click chemistry moiety selected from one of an azido group or an alkyne group and the label includes a click chemistry moiety selected from the other of the azido group or the alkyne group.5. The method of wherein the label includes a label selected from a biotin molecule claim 1 , a fluorescent molecule or a ...

Glycan arrays and method of use

The invention relates to linkers and methods for generating arrays with linkers. The invention also relates to methods for identifying agents that bind to various types of molecules on the arrays and to defining the structural elements of the molecules on the arrays that bind to those agents. The arrays and methods provided herein may be used for epitope identification, drug discovery and as analytical tools. The invention provides useful glycans and epitope determinants that are useful in detecting, diagnosing, recurrence monitoring and preventing cancer.

Neutralizing antibodies to ebola virus glycoprotein and their use

Antibodies and antigen binding fragments that specifically bind to ebolavirus glycoprotein and neutralize ebolavirus infection are disclosed. Nucleic acids encoding these antibodies, vectors, and host cells are also provided. The disclosed antibodies, antigen binding fragments, nucleic acids and vectors can be used, for example, to inhibit an ebolavirus infection in a subject.

Stimuli-responsive surfaces

A stimuli-responsive surface (3) comprising a substrate (20) on which is located a switchable molecule (2) which has a functional moiety (22) associated therewith, wherein the switchable molecule (2) has a first equilibrium state (2A) in which access to the functional moiety (22) is inhibited and a second stimulated state (2B), in which access to the functional moiety (22) is permitted.

BIOMARKERS FOR ASSESSMENT OF PREECLAMPSIA

Disclosed herein are screening tools for fetal/maternal wellness, such as biomarkers for assessing preeclampsia. More specifically, methods are disclosed for assessing the risk of preeclampsia in a subject, the methods including obtaining a first serum sample from the subject, determining a level of glycosylated fibronectin (GlyFn) in the first serum sample, and comparing the determined level of GlyFn with a control value, wherein an elevation in the determined level of GlyFn in the first serum sample relative to the control value indicates that the subject is at increased risk of preeclampsia. Also disclosed are methods of determining the risk of preeclampsia in a subject during a first, second, or third trimester, methods of assessing severity and progression of preeclampsia and complications of a risk of low birth weight or HELLP syndrome. 2. The method of claim 1 , further comprising:if preeclampsia is diagnosed in the subject, preparing the subject for delivery, or performing an additional test on the subject.3. The method of claim 1 , wherein the method further includes selecting a subject at risk for preeclampsia.4. The method of claim 1 , wherein determining whether the measured level of GlyFn is elevated relative to the GlyFn control value comprises determining whether the measured level of GlyFn is at least 15% higher than the GlyFn control value.5. The method of claim 1 , wherein determining whether the measured level of GlyFn is elevated relative to the GlyFn control value comprises determining whether the measured level of GlyFn is at least 30% higher than the GlyFn control value.6. The method of claim 1 , wherein determining whether the measured level of GlyFn is elevated relative to the GlyFn control value comprises determining whether the measured level of GlyFn is at least 50% higher than the GlyFn control value.7. The method of claim 1 , wherein determining whether the measured level of GlyFn is elevated relative to the GlyFn control value ...

NOVEL ANTI-LAM AND ANTI-PIM6/LAM MONOCLONAL ANTIBODIES FOR DIAGNOSIS AND TREATMENT OF MYCOBACTERIUM TUBERCULOSIS INFECTIONS

The present invention broadly provides different compositions, kits, vectors, and methods including monoclonal antibodies directed to epitopes found within lipoarabinomannan (LAM) and phosphatidyl-myo-inositol mannoside 6 (PIM6) for the diagnosis and treatment of infections. 1. A monoclonal anti-lipoarabinomannan (anti-LAM) antibody , or an antigen-binding portion thereof , that specifically binds to a LAM epitope comprising an Ara4 structure , an Ara6 structure , or a combination thereof , wherein the anti-LAM antibody comprises a CDR1 light chain variable region having at least 80% identity with SEQ ID NO: 1 or antigenic fragments thereof , a CDR2 light chain variable region having at least 80% identity with SEQ ID NO: 2 or antigenic fragments thereof , a CDR3 light chain variable region having at least 80% identity with SEQ ID NO: 3 or SEQ ID NO: 26 or antigenic fragments thereof , a CDR1 heavy chain variable region having at least 80% identity with SEQ ID NO: 4 or antigenic fragments thereof , a CDR2 heavy chain variable region having at least 80% identity with SEQ ID NO: 5 or antigenic fragments thereof , and a CDR3 heavy chain variable region having at least 80% identity with SEQ ID NO: 6 or SEQ ID NO: 23 or antigenic fragments thereof.2. The monoclonal anti-LAM antibody or antigen-binding portion thereof of claim 1 , said antibody comprising a heavy chain variable region comprising the amino acid sequences of SEQ ID NO:21 and SEQ ID NO:23 claim 1 , and a light chain variable region comprising the amino acid sequences of SEQ ID NO: 24 and SEQ ID NO:26.3. The monoclonal anti-LAM antibody or antigen-binding portion thereof of claim 1 , wherein the antibody is an scFv-IgG claim 1 , an IgA or an IgM antibody.4. The monoclonal anti-LAM antibody or antigen binding portion thereof of claim 1 , wherein the antibody is a human antibody claim 1 , a humanized antibody claim 1 , or a chimeric antibody.5. A method of diagnosing an active tuberculosis infection in an ...

METHOD FOR MEASURING GLYCOPROTEIN, METHOD FOR EXAMINING LIVER DISEASE, REAGENT FOR QUANTITATIVE DETERMINATION OF GLYCOPROTEIN, AND GLYCAN-MARKER GLYCOPROTEIN AS AN INDEX FOR CLINICAL CONDITIONS OF LIVER DISEASE

An object of the present invention is to provide a method for measuring a glycan-marker glycoprotein, by which liver disease can be detected with higher accuracy than is possible with conventional methods. Also, an object of the present invention is to provide a method for examining liver disease, by which liver disease can be detected with higher accuracy than is possible with conventional methods. Also, an object of the present invention is to provide a reagent for quantitative determination of a glycoprotein, which is used for the above measurement methods. Furthermore, an object of the present invention is to provide a glycan-marker glycoprotein as an index for clinical conditions of liver disease, which is capable of identifying the clinical conditions of liver disease depending on the progress of liver disease. The method for measuring a glycoprotein is characterized in that: the glycoprotein is at least one glycoprotein selected from alpha-1-acid glycoprotein (AGP) and Mac-2-binding protein (M2BP) contained in a sample collected from a subject; when the glycoprotein is AGP, AGP binding to a first lectin selected from AOL and MAL is measured; and when the glycoprotein is M2BP, M2BP binding to a second lectin selected from WFA, BPL, AAL, RCA120, and TJAII is measured. 130-. (canceled)31. A method for detecting cirrhosis , comprising:{'i': 'Wisteria floribunda', 'mixing a blood sample collected from a patient with liver disease, a lectin (WFA) and an anti-Mac-2-binding protein antibody;'}assaying Mac-2-binding protein (M2BP) binding to both the WFA and the anti-M2BP antibody; anddetermining whether or not the liver disease is cirrhosis based on the assayed value of the M2BP.32. The method according to claim 31 , wherein the blood sample is a serum.33. The method according to claim 31 , wherein the mixing is performed by mixing the blood sample and the WFA claim 31 , and mixing the M2BP antibody and a mixture of the blood sample and the WFA.34. The method ...

A-FUCOSYLATION DETECTION IN ANTIBODIES

This invention describes a new analytical method to determine the quantity and distribution of fucose per Fc within an antibody preparation. 1. A method for preparing a homogenously deglycosylated immunoglobulin G antibody or a homogenously deglycosylated Fc fragment thereof , the method comprising(a) providing an antibody preparation, wherein the antibody preparation comprises a glycosylated immunoglobulin G antibody or a glycosylated Fc fragment thereof, and(b) removing heterogeneous saccharide residues from the glycosylated immunoglobulin G antibody or the glycosylated Fc fragment thereof with the enzyme endoglycosidase S and the enzyme endoglycosidase H, thereby preparing a homogenously deglycosylated immunoglobulin G antibody or a homogenously deglycosylated Fc fragment thereof.2. The method of claim 1 , wherein the enzyme endoglycosidase S cleaves complex-type N-linked carbohydrate moieties from the glycosylated immunoglobulin G antibody or the glycosylated Fc fragment thereof claim 1 , and the enzyme endoglycosidase H cleaves hybrid-type N-linked carbohydrate moieties from the glycosylated immunoglobulin G antibody or the glycosylated Fc fragment thereof.3. The method of claim 1 , wherein the method further comprises detecting the presence or absence of fucose residues within the homogenously deglycosylated immunoglobulin G antibody or the homogenously deglycosylated Fc fragment thereof claim 1 , the method comprising(a) removing other heterogeneous residues from the homogenously deglycosylated immunoglobulin G antibody or the homogenously deglycosylated Fc fragment thereof with an enzyme, and(b) analyzing the immunoglobulin G antibody or the Fc fragment thereof for the presence or absence of fucose residues.4. The method of claim 3 , wherein the method further comprises purifying the homogenously deglycosylated immunoglobulin G antibody or the homogenously deglycosylated Fc fragment thereof prior to analyzing the immunoglobulin G antibody or the Fc fragment ...

Dna-glycan conjugates and methods of use

Provided herein are DNA-glycan conjugates that include a glycan and a covalently attached polynucleotide. The polynucleotide includes a plurality of modules. Each module includes a nucleotide string, and the plurality of modules includes a monomer module that corresponds to each carbohydrate monomer present in the DNA-glycan conjugate, and a linkage module that corresponds to each glycosidic linkage present between each carbohydrate monomer in the DNA-glycan conjugate. The nucleotide sequence of the plurality of modules corresponds to the glycan structure. Also provided herein are methods for making and using the DNA-glycan conjugates. Further provided is a computer-implemented method for translating data from a nucleotide sequence to a glycan structure, a system for converting data from a glycan structure to a nucleotide sequence, and a system for translating data from a nucleotide sequence to a glycan structure.

Sandwich assay using labeled lectin and kit therefor

The present invention provides a sandwich assay for quantifying a glycoprotein, which is a substance to be detected, in a sample using a labeled lectin, wherein the effect attributed to a contaminant, namely noise on the quantified value of the substance to be detected, is suppressed by introduction of a simple treatment. The sandwich assay includes a treatment for inhibiting the binding of the labeled lectin to a sugar chain carried by the contaminant non-specifically adsorbed to the measurement region, which contaminant is contained in the sample and which sugar chain is the same as that of the substance to be detected.

GLYCAN-INTERACTING COMPOUNDS

The present invention provides glycan-interacting antibodies useful in the treatment and prevention of human disease, including cancer. Such glycan-interacting antibodies include monoclonal antibodies, derivatives and fragments thereof as well as compositions and kits comprising them. 1. A method of treating cancer comprising administering a glycan-interacting antibody to a subject in need thereof , said glycan-interacting antibody comprising a heavy chain variable domain (VH) with the amino acid sequence of SEQ ID NO: 1 and a light chain variable domain (VL) with the amino acid sequence of SEQ ID NO: 2.2. The method of claim 1 , wherein said glycan-interacting antibody targets a cancer-related antigen.3. The method of claim 2 , wherein said cancer-related antigen comprises at least one glycan claim 2 , said at least one glycan comprising at least one sialic acid residue.4. The method of claim 3 , wherein said at least one glycan comprises at least one of Neu5Gcα2 claim 3 ,6GalNAc; Neu5Gcα2 claim 3 ,6Galβ1 claim 3 ,4GlcNAc; Neu5Gcα2 claim 3 ,6Galβ1 claim 3 ,4Glc; and Neu5Gcα2 claim 3 ,6Gal.5. The method of claim 3 , wherein said at least one glycan comprises a 9-O-acetylated glycan.6. The method of claim 5 , wherein said 9-O-acetylated glycan is one of Neu5Gc9Acα2 claim 5 ,6Galβ1 claim 5 ,4GlcNAc; Neu5Gc9Acα2 claim 5 ,6GalNAc; Neu5Gc9Acα2 claim 5 ,6Gal; and Neu5Gc9Acα2 claim 5 ,6Galβ1 claim 5 ,4Glc.7. A method of delivering a payload to a cell claim 5 , the method comprising contacting said cell with a glycan-interacting antibody claim 5 , said glycan-interacting antibody comprising a heavy chain variable domain (VH) with the amino acid sequence of SEQ ID NO: 1 and a light chain variable domain (VL) with the amino acid sequence of SEQ ID NO: 2 claim 5 , and wherein said payload is attached to said glycan-interacting antibody.8. The method of claim 7 , wherein the payload is conjugated to the glycan-interacting antibody prior to contacting said cell.9. The method of ...

High-affinity mycobacterium tuberculosis capsule-specific human monoclonal antibody

Provided are high affinity Mycobacterium tuberculosis capsule-specific antibodies and fragments thereof, as well as methods of use and devices employing such antibodies and/or fragments.

Kit-of-parts to identify mother's milk missing fucosyltransferase-2 dependent glycans and feeding doses with said glycans

Described is a matrix to identify mother's milk missing fucosyltransferase-2 (FUT2) dependent glycans which comprise a line of a glycan binding protein such as a lectin or antibody suitable to bind 2′fucosyl-glycans and a line of a positive control to bind a mother's milk protein. For instance, this matrix is porous and allows for transport by capillary force of compounds of mother's milk such as glycoproteins. Especially, the glycan binding protein is the plant lectin from Ulex europaeus. A diagnostic kit comprising one or more of such matrices and a device suitable to receive such a matrix provided with a milk application window and a read-out window has been described as well. Finally a kit-of-parts comprising such a diagnostic kit and one or more feeding doses of 2′fucosyl-glycans has been disclosed.

METHODS AND KITS FOR CANCER ANTIGEN AND HEPARAN SULFATE IMAGING

An in vitro method of imaging a cancer antigen includes providing a cell sample including a cancer antigen selected from the group consisting of a Tn antigen, a T antigen, a sialylated-Tn antigen, and a sialylated-T antigen, treating the sample with a glycosyltransferase to incorporate a carbohydrate with a click chemistry moiety into the cancer antigen, adding a label to the sample that includes a click chemistry moiety that reacts to the click chemistry moiety of the carbohydrate such that the label attaches to the carbohydrate to form a labeled cancer antigen, and imaging the sample with a camera. 1. An in vitro method of imaging a cancer antigen , the method comprising:providing a sample comprising a cancer antigen selected from the group consisting of a Tn antigen, a T antigen, a sialylated-Tn antigen, and a sialylated-T antigen;treating the sample with a glycosyltransferase to incorporate a carbohydrate into the cancer antigen, wherein the carbohydrate includes a click chemistry moiety;adding a label to the sample, wherein the label includes a click chemistry moiety that reacts to the click chemistry moiety of the carbohydrate such that the label attaches to the carbohydrate to form a labeled cancer antigen; andimaging the sample with a camera.23613132616264. The method of claim 1 , wherein the glycosyltransferase is selected from the group consisting of BGNT claim 1 , GCNT claim 1 , STGal claim 1 , STGal claim 1 , STGalNAc claim 1 , STGalNAc claim 1 , and STGalNAc.3. The method of claim 1 , further comprising treating the sample with sialidase prior to treating the sample with the glycosyltransferase to expose a glycosyltransferase recognition site.4. The method of claim 1 , wherein the label is a fluorescent label claim 1 , a colorimetric label claim 1 , a biotin linked to a fluorescent label claim 1 , or a biotin linked to a colorimetric label claim 1 , and wherein the carbohydrate includes a click chemistry moiety selected from one of an azido group or an ...

OPTIMIZING DIAGNOSTICS FOR GALACTOFURANOSE CONTAINING ANTIGENS

Disclosed herein are methods of detecting microbial infection in mammalian subjects comprising treatment of a sample and detection of galactofuranose (galF)-containing antigenic components utilizing monoclonal antibodies. The methods disclosed provide for pretreatment of biological samples, such as urine samples, to maximize detection of galF antigens and improvement of sensitivity of galF antigen detection assays. The methods include minimizing intelectin-1 binding to galF antigens and improvement of monoclonal antibody binding. The detection methods are useful for identifying the presence of microbial antigens related to bacterial, fungal, and parasitic pathogens, including species, species, species, species, species, and species. 1. A method for diagnosing a microbial infection in a biological sample from a mammalian subject suspected of having , having , or susceptible to having a microbial infection by detecting the presence of at least one polysaccharide comprising a galactofuranose residue in a biological sample of the mammalian subject , the method comprising:(a) treating the biological sample to inhibit human intelectin (hIntL) binding of galactofuranose residues present in the sample;(b) contacting the treated sample of (a) with at least one antibody specific for at least one polysaccharide comprising a galactofuranose residue in an effective amount to produce a detectable amount of antibody-polysaccharide complex; and(c) detecting the presence of at least one antibody-polysaccharide complex, wherein the detection of the presence of at least one antibody-polysaccharide complex is diagnostic of a microbial infection in a mammalian subject.2. The method of claim 1 , wherein in step (a) treating the sample comprises contacting the sample with a substrate.3. The method of claim 2 , wherein the substrate comprises a polyacrylamide resin.4. The method of claim 2 , wherein the substrate comprises a desalting column.5. The method of claim 4 , wherein the desalting ...

Anti-MUC1 Antibody or Antigen-Binding Fragment Thereof and Uses Thereof

The present invention provides: an antibody exhibiting specificity for MUC1, the antibody having a glycan structure expressed at high levels in cancer cells; a method for manufacturing this antibody; and a novel means and method for the diagnosis and prevention and/or treatment of cancer using this antibody. The present invention is a monoclonal antibody to human MUC1, wherein the antibody specifically recognizes a glycopeptide having a human MUC1 tandem unit and furthermore having an O-linked glycan core (0(Tn)) in any one of the threonine and serine in the amino acid sequence of this human MUC1 tandem unit. A method for detecting MUC1 in a human body-fluid sample. A kit including this monoclonal antibody. A pharmacological composition for the prevention and/or treatment of a malignant tumor, the pharmacological composition containing this monoclonal antibody as an active ingredient.

Immunomodulating compositions and methods of use thereof

The invention is directed to β1-6 glucans, compositions, diagnostic kits, and devices comprising the same, and methods of use thereof in modulating immune response and treating, delaying progression of, reducing the incidence or severity of cancer, infection, inflammation, and autoimmune diseases. The β1-6 glucans of certain embodiments of the invention are enriched for O-acetylated groups and/or conjugated to a solid support or linked to a targeting moiety. The β1-6 glucans of certain embodiments of the invention recruit immunoglobulin G antibodies to mediate complement and neutrophil killing. The conjugated β1-6 glucans of certain embodiments of the invention are targeted to cells to stimulate the immune response at the target location by activating complement-mediated lysis and recruitment of neutrophils.

Methods of Detecting Conjugation Site-Specific and Hidden Epitope/Antigen

This invention discloses “Artificially Cleaved Epitope (ACE)” methods, antibodies, reagents, immunoassays, and kits for designing and detecting hidden epitopes/antigens. The ACE methods can detect epitopes that are either absent or poorly accessible naturally to antibodies, and thus must be specifically and artificially created (free terminals) and/or exposed in samples and sample preparations for antibody detection. The ACE structures include, but are not limited to, macromolecule-to-macromolecule conjugation sites, and any types of linear hidden epitopes. The ACE methods comprise ACE antigen design and ACE antigen detection. The ACE methods, antibodies, reagents, immunoassays, and kits are useful in research and discovery, diagnostic, and therapeutic applications. In another aspect, the ACE methods can artificially and specifically expose hidden antigens while reducing the antibody non-specific bindings in all antibody-based applications. 1. A method of detecting a hydrolysis-created Artificially Cleaved Epitope (ACE) structure in a sample , wherein the ACE structure is hidden in its intact or natural form in a polymeric molecule and is poorly accessible to antibodies , comprising steps of:(i) designing an ACE structure of formula L1-L2---Ln, wherein L1 and Ln are each terminal residues that are artificially created via chemical bond-specific cleavage by a hydrolytic enzyme or hydrolytic agent, wherein the antibody specifically recognizes at least one of the L1 or Ln terminal residues or residues between L1 and Ln;(ii) synthesizing the ACE structure;(iii) making an antibody against the ACE structure;(iv) creating the ACE structure in the sample by treating the sample preparation with the hydrolytic enzyme or hydrolytic agent thereby exposing the formerly hidden ACE. structure to specific interaction with the antibody; and(v) detecting the ACE structure created in step (iv) with the antibody, wherein the antibody specifically binds to at least one of the ...

Optimizing diagnostics for galactofuranose containing antigens

Disclosed herein are methods of detecting microbial infection in mammalian subjects comprising treatment of a sample and detection of galactofuranose (galF)-containing antigenic components utilizing monoclonal antibodies. The methods disclosed provide for pretreatment of biological samples, such as urine samples, to maximize detection of galF antigens and improvement of sensitivity of galF antigen detection assays. The methods include minimizing intelectin-1 binding to galF antigens and improvement of monoclonal antibody binding. The detection methods are useful for identifying the presence of microbial antigens related to bacterial, fungal, and parasitic pathogens, including Streptococcus pneumoniae, Aspergillus species, Fusarium species, Coccidioides species, Cryptococcus species, Histoplasma species , and Leishmania species.

Method, kit and device for preparing glycoprotein sugar chain

Provided is a method for preparing a glycoprotein sugar chain including: an isolation step of acting a sugar chain-isolating enzyme on a sample which contains a glycoprotein fixed to a solid phase in a container to obtain an isolated product which contains a sugar chain; and a labeling step of adding a labeling reagent to the isolated product in the container to obtain a labeled product which contains a labeled substance of the sugar chain.

METHOD AND KIT FOR DISTINGUISHING BETWEEN PROSTATE CARCINOMA AND BENIGN PROSTATIC HYPERPLASIA

An object of the present invention is to provide a method for distinguishing between prostate carcinoma and benign prostatic hyperplasia with high sensitivity and good reproducibility using a small amount of an analyte sample. The method for distinguishing between prostate carcinoma and benign prostatic hyperplasia according to the present invention as a solution means thereof comprises: bringing an analyte sample containing a prostate-specific antigen (PSA) into contact with a carrier having an anti-free PSA antibody immobilized thereon, thereby binding free PSA to the anti-free PSA antibody immobilized on the carrier; thereafter bringing the carrier in which the free PSA is bound to the immobilized anti-free PSA antibody into contact with a monoclonal antibody capable of specifically recognizing a glycan in which a terminal sialic acid residue is bound to galactose through an α(2,3) bond, thereby binding the monoclonal antibody capable of specifically recognizing a glycan in which a terminal sialic acid residue is bound to galactose through an α(2,3) bond to the free PSA bound to the anti-free PSA antibody immobilized on the carrier; measuring the amount of the free PSA having an N-type glycan in which a terminal sialic acid residue is bound to galactose through an α(2,3) bond; comparing the measured amount thus obtained with a preset cutoff value for prostate carcinoma and benign prostatic hyperplasia, thereby determining that when the measured amount is larger than the cutoff value, prostate carcinoma is developed or the probability of developing prostate carcinoma is high, and when the measured amount is smaller than the cutoff value, benign prostatic hyperplasia is developed or the probability of developing benign prostatic hyperplasia is high. 1. A method for distinguishing between prostate carcinoma and benign prostatic hyperplasia , comprising: bringing an analyte sample containing a prostate-specific antigen (PSA) into contact with a carrier having an anti ...

SACCHARIDE-BASED BIOMARKERS AND THERAPEUTICS

The invention provides antibodies that specifically bind to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine expressed by a cancer cell or an inflammatory cell. Also provided are compositions including these antibodies, as well as polynucleotides, vectors, host cells, and methods useful for production thereof. Further provided are methods and kits for treating or preventing cancer in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine, optionally in combination with another anti-cancer agent. Still further provided are methods and kits for treating or preventing gastrointestinal disease in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine. Yet further provided are methods and kits for detecting the presence of cancer cells in an individual including an antibody that specifically binds to an epitope containing N-acetylglucosamine and/or N-acetyl-galactosamine. 129-. (canceled)30. An isolated polynucleotide comprising a nucleic acid sequence encoding an isolated monoclonal antibody , which antibody specifically binds to an epitope comprising N-acetylglucosamine or N-acetyl-galactosamine , wherein the epitope is expressed by a cancer cell or an inflammatory cell , and wherein the antibody comprises:(a) a heavy chain variable region comprising three HVRs from the amino acid sequence of SEQ ID NO:1, and a light chain variable region comprising three HVRs from the amino acid sequence of SEQ ID NO:2;(b) a heavy chain variable region comprising three HVRs from the amino acid sequence of SEQ ID NO:3, and a light chain variable region comprising three HVRs from the amino acid sequence of SEQ ID NO:4;(c) a heavy chain variable region comprising three HVRs from the amino acid sequence of SEQ ID NO:5, and a light chain variable region comprising three ...

METHOD FOR DETERMINING A LECTIN-BINDING GLYCAN INDICATIVE TO TRAUMATIC BRAIN INJURY

The present invention relates to a method for determining a lectin-binding glycan indicative to traumatic brain injury (TBI) wherein the determining is based on detection of the lectin-binding glycan in a fluid sample using lectins of similar glycan binding property for tracing and capturing. 1. A method for determining a lectin-binding glycan indicative to traumatic brain injury (TBI) in a fluid sample , the method comprising [ a first part, a second part and a detection zone therebetween and', 'a first lectin adapted to bind the lectin-binding glycan and being immobilized to the detection zone, and, 'i. a probe comprising a porous matrix, the porous matrix comprising'}, a second lectin adapted to bind the lectin-binding glycan and', 'a signal generation means adapted to produce a detectable signal upon binding of the second lectin of the conjugate to the lectin-binding glycan immobilized to the detection zone via the first lectin,, 'ii. a conjugate comprising'}], 'a) providing'}wherein the first lectin and the second lectin have similar glycan-binding properties,b) exposing the detection zone to the fluid sample,c) exposing the detection zone to the conjugate,d) detecting signal derived from the signal generation means at the detection zone, ande) determining level of the lectin-binding glycan in the fluid sample based on the detecting.2. The method according to comprisingf) comparing the level of the lectin-binding glycan in the fluid sample to a control level indicative to a level of the lectin-binding glycan in body fluid of a subject not suffering from TBI andg) determining presence or absence of increased level of the lectin-binding glycan in the fluid sample based on the comparing.3. The method according to comprising removing unbound material from the detection zone before the detecting of step d).4. The method according to wherein the exposing of step b) comprises applying the fluid sample onto to the detection zone.5. The method according to wherein the ...

Brassica gat event and compositions and methods for the identification and/or detection thereof

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

Cleavage of Fucose in N-Glycans

Provided herein is an α-fucosidase that can cleave a conjugate comprising an N-glycan and a label where the label is added by amine reactive chemistry. The α-fucosidase also has an accelerated reaction time using Schiff base labeled N-glycans compared with BKF. A reaction mix, enzyme mix and kit comprising the α-fucosidase are provided, as well as a method for analyzing glycoproteins. The α-fucosidase finds particular use in analyzing the N-glycans of therapeutic glycoproteins. 1. A reaction mix comprising:(a) an α-L-fucosidase having an amino acid sequence that is at least 90% identical to amino acids 23-359 of sequence of SEQ ID NO:1 ; and(b) a conjugate comprising an N-glycan and a label.2. The reaction mix of claim 1 , wherein the label comprises a fluorophore and/or a charge tag.3. The reaction mix of claim 1 , wherein the N-glycan of the conjugate comprises a core fucose.4. The reaction mix of claim 1 , wherein the N-glycan is linked to the label via the reducing end of the N-glycan.5. The reaction mix of claim 1 , wherein the N-glycan is linked to the label via amine reactive chemistry or by a Schiff base condensation reaction.6. The reaction mix of claim 1 , wherein the N-glycan is from a therapeutic glycoprotein.7. The reaction mix of claim 1 , wherein the reaction mix further comprises: α2-3 neuraminidase S,', 'α2-3,6,8,9 neuraminidase A,', 'α1-3,4,6 galactosidase,', 'β1-4 galactosidase,', 'β-N-acetylglucosaminidase S, and', 'α1-2,3,6 mannosidase., '(c) one or more exoglycosidases selected from the group consisting of8. The reaction mix of claim 1 , wherein the reaction mix has a pH in the range of pH 3.0 to pH 5.5.9. An enzyme mix comprising:(a) an α-fucosidase having an amino acid sequence that is at least 90% identical to amino acids 23-359 of sequence of SEQ ID NO:1; and α2-3 neuraminidase S,', 'α2-3,6,8,9 neuraminidase A,', 'α1-3,4,6 galactosidase,', 'β1-4 galactosidase,', 'β-N-acetylglucosaminidase S, and', 'α1-2,3,6 mannosidase., '(b) one or more ...

BIOMARKERS TO DETECT AND CHARACTERISE CANCER

Disclosed herein are methods of detecting the presence or absence of cancer. Also disclosed herein are methods of characterising a sample from a subject thought to be suffering cancer, as well as methods of determining the malignancy, grade, or staging of a cancer. Also disclosed herein are kits utilising the methods disclosed herein. 1. A method of detecting the presence or absence of cancer ,wherein the method comprises the steps of:(i) obtaining a sample from a subject;(ii) detecting a level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in the sample obtained in step (i);(iii) comparing the level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in step (ii) with a level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in a control group;wherein an increase in the level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins present in the sample compared to the control group is indicative of the presence of cancer.2. A method of determining the risk of a subject developing cancer , wherein the method comprises the steps of:(i) obtaining a sample from a subject;(ii) detecting a level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in the sample;(iii) comparing the level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in step (ii) with a level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins in a control group;wherein an at least 4-fold increase in the level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins present in the sample compared to the control group is indicative that the subject is suffering from cancer.3. The method according to claim 1 , wherein the detection of the level of O-glycosylation of one or more endoplasmic reticulum (ER)-resident proteins comprises contacting the sample with a monosaccharide-binding protein.4. ...

BORRELIA BURGDORFERI PEPTIDOGLYCAN AS A DIAGNOSTIC AND TARGET FOR THERAPEUTIC INTERVENTION OF LYME DISEASE-RELATED PATHOLOGIES

The present disclosure relates to a method of diagnosing Lyme disease in a subject comprising measuring the level of peptidoglycan or the level of an antibody that specifically binds to peptidoglycan (“anti-peptidoglycan agent”). The present disclosure also relates to a method of treating a Lyme disease in a subject in need thereof comprising administering to the subject an antagonist against peptidoglycan (e.g., an anti-peptidoglycan antibody or a peptidoglycan-specific hydrolase). Antagonists (e.g., anti-peptidoglycan antibodies) suitable for the present methods are also disclosed. 1Borrelia burgdorferiBorrelia burgdorferi. A method of diagnosing Lyme disease in a subject in need thereof comprising contacting an antibody or innate immunity protein that specifically binds to peptidoglycan (“anti-peptidoglycan agent”) with a biological sample of the subject and measuring the level of peptidoglycan in the sample.2Borrelia burgdorferi. The method of claim 1 , wherein the biological sample of the subject has a greater level of peptidoglycan compared to a reference control sample.3B. burgdorferi. The method of or claim 1 , wherein the level of peptidoglycan in the biological sample of the subject is greater than at least about 5% claim 1 , at least about 10% claim 1 , at least about 20% claim 1 , at least about 30% claim 1 , at least about 40% claim 1 , at least about 50% claim 1 , at least about 60% claim 1 , at least about 70% claim 1 , at least about 80% claim 1 , at least about 90% claim 1 , at least about 100% claim 1 , at least about 150% claim 1 , at least about 200% claim 1 , at least about 300% or more compared to a corresponding level in the reference sample.4B. burgdorferi. A method of diagnosing Lyme disease in a subject in need thereof comprising contacting an anti-idiotypic antibody with a biological sample of the subject and measuring the level of the anti-idiotypic antibody in the sample claim 1 , wherein the anti-idiotypic antibody binds to a region of ...

GLYCAN-INTERACTING COMPOUNDS

The present invention provides glycan-interacting antibodies useful in the treatment and prevention of human disease, including cancer. Such glycan-interacting antibodies include monoclonal antibodies, derivatives and fragments thereof as well as compositions and kits comprising them. 1. A method of producing a glycan-interacting antibody comprising:i. contacting one or more mammals with a composition comprising submaxillary mucin and an adjuvant;ii. obtaining one or more serum samples from said one or more mammals;iii. characterizing the binding specificity and/or binding affinity of one or more antibodies present in said one or more serum samples for one or more glycans;iv. selecting at least one mammal determined to have serum antibodies with desired binding specificity and/or binding affinity for said one or more glycans; andv. establishing hybridoma cells using spleen cells from said at least one mammal and culturing said hybridoma cells to produce said glycan-interacting antibody.2. The method of claim 1 , wherein characterizing the binding specificity and/or binding affinity of one or more antibodies in said one or more serum samples for one or more glycans is carried out using at least one of an enzyme-linked immunosorbent assay (ELISA) and a glycan array.3. The method of claim 2 , wherein said glycan array comprises at least one glycan selected from Neu5Ac-α-2-6-GalNAc (AcSTn) claim 2 , Neu5Gc-α-2-6-GalNAc (GcSTn) claim 2 , Neu5 claim 2 ,9Ac2-α-2 claim 2 ,6-GalNAc claim 2 , Neu9Ac5Gc-α-2 claim 2 ,6-GalNAc claim 2 , and GalNAc (Tn).4. The method of claim 1 , wherein said submaxillary mucin is selected from at least one of porcine submaxillary mucin (PSM) claim 1 , bovine submaxillary mucin (BSM) claim 1 , and ovine submaxillary mucin (OSM).5. The method of claim 1 , wherein said one or more glycans are selected from at least one of AcSTn and GcSTn.6. The method of claim 5 , wherein said desired binding specificity includes binding specificity for AcSTn over ...

NOVEL ANTI-LAM AND ANTI-PIM6/LAM MONOCLONAL ANTIBODIES FOR DIAGNOSIS AND TREATMENT OF MYCOBACTERIUM TUBERCULOSIS INFECTIONS

The present invention broadly provides different compositions, kits, vectors, and methods including monoclonal antibodies directed to epitopes found within lipoarabinomannan (LAM) and phosphatidyl-myo-inositol mannoside 6 (PIM6) for the diagnosis and treatment of infections. 1tuberculosis. A method of diagnosing an active infection in an individual comprising:(a) obtaining a sample from an individual that comprises or is suspected of comprising lipoarabinomannan (LAM);(b) contacting the sample with a first antibody that binds specifically to an epitope present on a LAM molecule;(c) contacting the sample with a detection antibody that binds specifically to a different binding site in the LAM molecule than the binding site bound by the first antibody;(d) detecting binding of the detection antibody to the different binding site in the LAM molecule; and{'i': 'tuberculosis', '(e) diagnosing the patient as having an active infection,'}{'i': 'tuberculosis', 'wherein capture of LAM by the first antibody indicates an active infection, and'}wherein at least one of the antibodies is a human monoclonal anti-LAM antibody, or an antigen-binding portion thereof, that specifically binds to a LAM epitope comprising an Ara4 structure, an Ara6 structure, or a combination thereof, wherein the anti-LAM antibody comprises a CDR1 light chain variable region having at least 80% identity with SEQ ID NO: 1 or antigenic fragments thereof, a CDR2 light chain variable region having at least 80% identity with SEQ ID NO: 2 or antigenic fragments thereof, a CDR3 light chain variable region having at least 80% identity with SEQ ID NO: 3 or SEQ ID NO: 26 or antigenic fragments thereof, a CDR1 heavy chain variable region having at least 80% identity with SEQ ID NO: 4 or antigenic fragments thereof, a CDR2 heavy chain variable region having at least 80% identity with SEQ ID NO: 5 or antigenic fragments thereof, and a CDR3 heavy chain variable region having at least 80% identity with SEQ ID NO: 6 or ...

Diagnostic Test for Hepatocellular Carcinoma

The present invention relates to a method for detecting fucosylated alpha1-acid glycoprotein (AGP) in a sample, comprising the steps providing a monovalent fucose-binding peptide having at least 80% identity, such as 85, 90, 95, 99 or 100% identity, to a peptide having an amino acid according to SEQ ID NO: 1, immobilised on a solid phase; bringing the sample into contact with the immobilised fucose-binding peptide; and detecting any fucosylated AGP bound to said fucose-binding peptide. The invention further relates to a method for assessing a risk that a human individual suffers from hepatocellular carcinoma, and to a kit of parts and antibodies useful in the methods according to the invention, and to a peptide useful as an immunizing antigen in production of such antibodies. 1. A method for detecting fucosylated alpha1-acid glycoprotein (AGP) in a sample , the method comprising:providing a monovalent fucose-binding peptide having at least 80% identity to a peptide having an amino acid sequence according to SEQ ID NO: 1, immobilised on a solid phase;bringing the sample into contact with the immobilised fucose-binding peptide; anddetecting fucosylated alpha1-acid glycoprotein (AGP) bound to said fucose-binding peptide.2. The method according to claim 1 , further comprising quantitating the amount of AGP in the sample.3. The method according to claim 1 , wherein the detection of bound fucosylated AGP is performed by bringing bound fucosylated AGP in contact with a first detection antibody capable of specific binding to a fucosylated AGP bound to said fucose-binding peptide.4. The method according to claim 3 , wherein the first detection antibody is specific for an epitope comprising amino acid residues 183-201 of human AGP (SEQ ID NO: 2).5. The method according to claim 4 , wherein the first detection antibody is conjugated to a detectable label.6. The method according to claim 3 , wherein the detection of fucosylated AGP bound to said fucose-binding peptide is ...

GLYCOCONJUGATES AND METHODS FOR THEIR USE

Certain embodiments are directed to method for synthesizing and using glycoconjugates on the immunodominant epitope Galα()Galβ(()GlcNAcα (GalαLNα). 1. A neoglycoconjugate comprising a trisaccharide coupled to a carrier.2. The neoglycoconjugate of claim 1 , further comprising a linker connecting the trisaccharide to the carrier.3. The neoglycoconjugate of wherein the carrier is a protein carrier.4. The neoglycoconjugate of claim 3 , wherein the protein carrier is bovine serum albumin.5. The neoglycoconjugate of claim 1 , wherein the carrier is peptide.6. The neoglycoconjugate of claim 5 , wherein the peptide is a T cell epitope.7. The neoglycoconjugate of claim 1 , wherein the trisaccharide comprises a terminal galactose residue.8. The neoglycoconjugate of claim 1 , wherein the trisaccharide is Galα(1 claim 1 ,3)Galβ(1 claim 1 ,4)GlcNAcα.9. The neoglycoconjugate of claim 1 , wherein the trisaccharide is Galα(1 claim 1 ,3)Galβ(1 claim 1 ,4)GlcNAcα and the carrier bovine serum albumin.10. A method for chemical synthesis of a mercaptopropyl glycoside comprising:(a) converting an acyl-protected allyl disaccharide to a trichloroacetimide donor;(b) glycosylating the trichloroacetimide donor with a allyl-glycoside donor forming a trisaccharide allyl-glycoside; and(c) derivatizing the trisaccharide allyl-glycoside to a mercaptopropyl glycoside.(d) conjugating the mercaptopropyl glycoside to a carrier forming a neoglycoconjugate.11. The method of claim 10 , wherein the disaccharide is Galα(1 claim 10 ,3)Galβ(1 claim 10 ,4).12. The method of claim 10 , wherein the allyl-glycoside donor is an allyl-GlcNAcα.13. The method of claim 10 , wherein the carrier is a protein carrier.14. The method of claim 13 , wherein the protein carrier is bovine serum albumin.15. The method of claim 14 , wherein the mercaptopropyl glycoside is a glycoside of Galα(1 claim 14 ,3)Galβ(1 claim 14 ,4)GlcNAcα.16. The method of claim 10 , wherein the acyl-protected allyl disaccharide is produced by:(i) p- ...

CARBOHYDRATE LIGANDS THAT BIND TO IGM ANTIBODIES AGAINST MYELIN-ASSOCIATED GLYCOPROTEIN

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substitutents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone. 2. The compound of of formula (I) or (II) wherein Z is unsubstituted or substituted phenyl.3. The compound of of formula (I) or (II) wherein Z is p-methoxyphenyl.4. The compound of of formula (I) wherein Z is p-methoxyphenyl.5. The compound of of formula (II) wherein Z is p-methoxyphenyl.7. The polymer according to wherein the polymer backbone is an α-amino acid polymer claim 6 , an acrylic acid or methacrylic acid polymer or copolymer claim 6 , or a N-vinyl-2-pyrrolidone-vinyl alcohol copolymer.8. The polymer according to wherein the polymer backbone is an α-amino acid polymer claim 6 , wherein the α-amino acid is lysine claim 6 , glutamic acid or aspartic acid.9. The polymer according to wherein the polymer backbone is poly-lysine.10. The polymer according to wherein the molecular weight of the polymer backbone is 1 claim 7 ,000 D to 300 claim 7 ,000 D.11. The polymer according to claim 6 , wherein the linker Z is aryl claim 6 , heteroaryl claim 6 , aryl-lower alkyl claim 6 , arylcarbonyl claim 6 , or heteroarylmethyl claim 6 , wherein aryl or heteroaryl is substituted by alkylene with 3 to 25 carbon atoms connecting to the polymer wherein optionally(a) one or more carbon atoms of alkylene are replaced by nitrogen carrying a hydrogen atom, and one of the adjacent carbon atoms is substituted by oxo, representing an amide function —NH—CO—; ...

IMMUNOASSAY METHOD LESS AFFECTED BY IMPURITIES

An object of the present invention is to provide a method of measuring the amount of a compound containing a sugar chain in a biological sample by a sandwich immunoassay method using a labeled lectin, which method is suitable for reduction of noise originating from impurities and determination of the exact amount of a target compound. 1. A method of measuring the amount of a target compound comprising a sugar chain in a biological sample by a sandwich immunoassay method using a labeled lectin (including cases where a target compound-capturing substance other than an antibody is used as a ligand) , said method comprising adding a sugar chain compound which competes (crosses) with impurities contained in said biological sample in binding with said labeled lectin.2. The method according to claim 1 , wherein claim 1 , when the dissociation constant between said sugar chain compound to be added and said labeled lectin and the dissociation constant between said target compound and said labeled lectin are defined as “x” and “a” claim 1 , respectively claim 1 , said x is in a range of x>a.3. The method according to claim 2 , wherein said compound comprising a sugar chain in said biological sample to be measured is a tumor marker.4. The method according to claim 3 , wherein the combination of said target compound claim 3 , said labeled lectin and said sugar chain compound to be added is any of the following combinations of (1) to (4):{'i': 'Trichosanthes japonica', '(1) said target compound is a prostate-specific antigen (PSA), said labeled lectin is lectin (TJA-II), and said sugar chain compound to be added is a fucose derivative or a galactose derivative;'}{'i': 'Wisteria floribunda', '(2) said target compound is a prostate-specific antigen (PSA), said labeled lectin is lectin (WFA), and said sugar chain compound to be added is a fucose derivative;'}{'i': 'Lens culinaris', '(3) said target compound is a-fetoprotein (AFP), said labeled lectin is lectin (LCA), and said sugar ...

Fucosylation and immune surveillance in melanoma

Disclosed are methods for treating a cancer and/or enhancing immune responses to infiltration of tumors comprising administering to a subject a fucose. Also disclosed herein are methods of detecting the presence of a sugar-modified protein (i.e., a glycosylated protein).

GLYCOCONJUGATES AND METHODS FOR THEIR USE

Certain embodiments are directed to method for synthesizing and using glycoconjugates based on the immunodominant epitope Galα(1,3)Galβ(1,4)GlcNAcα (Galα3LNα). 1. A neoglycoconjugate comprising a trisaccharide coupled to a carrier.2. The neoglycoconjugate of claim 1 , further comprising a linker connecting the trisaccharide to the carrier.3. The neoglycoconjugate of wherein the carrier is a protein carrier.4. The neoglycoconjugate of claim 3 , wherein the protein carrier is bovine serum albumin.5. The neoglycoconjugate of claim 1 , wherein the carrier is peptide.6. The neoglycoconjugate of claim 5 , wherein the peptide is a T cell epitope.7. The neoglycoconjugate of claim 1 , wherein the trisaccharide comprises a terminal galactose residue.8. The neoglycoconjugate of claim 1 , wherein the trisaccharide is Gal_α(1 claim 1 ,3)Galβ(1 claim 1 ,4)GlcNAcα.9. The neoglycoconjugate of claim 1 , wherein the trisaccharide is Galα(1 claim 1 ,3)Galβ(1 claim 1 ,4)GlcNAcα and the carrier bovine serum albumin.10. A method for chemical synthesis of a mercaptopropyl glycoside comprising:(a) converting an acyl-protected allyl disaccharide to a trichloroacetimide donor;(b) glycosylating the trichloroacetimide donor with a allyl-glycoside donor forming a trisaccharide allyl-glycoside; and(c) derivatizing the trisaccharide allyl-glycoside to a mercaptopropyl glycoside. (d) conjugating the mercaptopropyl glycoside to a carrier forming a neoglycoconjugate.11. The method of claim 10 , wherein the disaccharide is Galα(1 claim 10 ,3)Galβ(1 claim 10 ,4).12. The method of claim 10 , wherein the allyl-glycoside donor is an allyl-GlcNAcα.13. The method of claim 10 , wherein the carrier is a protein carrier.14. The method of claim 13 , wherein the protein carrier is bovine serum albumin.15. The method of claim 14 , wherein the mercaptopropyl glycoside is a glycoside of Galα(1 claim 14 ,3)Galβ(1 claim 14 ,4)GlcNAcα.16. The method of claim 10 , wherein the acyl-protected allyl disaccharide is ...

APOE MODIFICATIONS AND USES THEREOF

Provided herein are methods for detecting a cerebrospinal fluid-specific (CSF-specific) glycoform of Apolipoprotein E (APOE) in a subject. 1. A method of detecting a cerebrospinal fluid-specific (CSF-specific) glycoform of Apolipoprotein E (APOE) in a subject comprising:a) obtaining a plasma sample from the subject; andb) detecting a CSF-specific glycoform of APOE in the plasma sample.2. The method of claim 1 , further comprising determining the level of the CSF-specific glycoform of APOE and/or the glycosylation pattern of the CSF-specific glycoform of APOE in the plasma sample.3. The method of claim 1 , wherein the subject has at least one copy of the APOE4 allele.4. The method of claim 1 , wherein the subject lacks copies of the APOE4 allele.5. The method of claim 1 , wherein the CSF-specific glycoform of APOE is an APOE glycoform that differs in glycosylation as compared to a control plasma-specific glycoform of APOE.6. The method of claim 1 , wherein the CSF-specific glycoform of APOE is an APOE glycoform that differs in glycosylation as compared to a control CSF-specific glycoform of APOE.7. The method of claim 5 , wherein the difference in glycosylation is a difference in the glycosylation pattern of the CSF-specific APOE glycoform.8. The method of claim 7 , wherein the difference in the glycosylation pattern is a difference in the number of glycosylated O-linked glycosylation sites claim 7 , a difference in the type of O-glycan at one or more glycosylation sites claim 7 , a difference in the amount of glycosylation at one or more O-linked glycosylation sites and/or a difference in sialylation at one or more O-linked glycosylation sites.9. The method of claim 8 , wherein the difference in the glycosylation pattern is a difference in the amount of glycosylation claim 8 , type of O-glycan claim 8 , and/or amount of sialyation at Thr8 claim 8 , Thr18 claim 8 , Thr194 claim 8 , Ser197 claim 8 , Thr289 claim 8 , Ser290 and/or Ser296 of the CSF-specific APOE ...

Marker for diabetic complications

An objective is to provide a marker that enables a diabetic complication to be examined. There is provided the marker for examining a diabetic complication, comprising a compound represented by the following Formula (1), or a salt thereof.

DETECTING CANCER STEM CELLS USING A GLYCAN BIOMARKER

Embodiments in accordance with the present disclosure include apparatuses, devices, and methods. An example method is directed to detecting cancer stem cells (CSCs) in a biological sample of a subject. The method includes causing a physical interaction between the biological sample and an antibody by exposing the biological sample to the antibody and determining a presence of CSCs in the biological sample by detecting binding between the antibody and a glycan biomarker. The glycan biomarker includes at least one chain selected from the group consisting of polylactosamine chains, oligosaccharide chains, and combinations thereof, the at least one chain having branches selected from the group consisting of IIβ (Galβ1,4GlcNAcβ1,6), IIβ/Iβ (Gal β1,3GlcNAc β1,6), IIβ/Iβ (Gal β1 4/3GlcNAc β1,6)-moieties, and combinations thereof. 1. A method for detecting cancer stem cells (CSCs) in a biological sample of a subject , the method comprising:causing a physical interaction between the biological sample and an antibody by exposing the biological sample to the antibody; and 'polylactosamine chains, oligosaccharide chains, and combinations thereof, the at least one chain having branches selected from the group consisting of: III (Galβ1,4GlcNAcβ1,6), Iβ(Galβ1,3GlcNAcβ1,6), IIβ/Iβ (Gal β1, 4/3GlcNAc β1,6)-moieties, and combinations thereof.', 'determining a presence of CSCs in the biological sample by detecting binding between the antibody and a glycan biomarker, the glycan biomarker including at least one chain selected from the group consisting of2. The method of claim 1 , wherein the glycan biomarker includes an epitope of a blood group precursor antigen and the antibody is an anti-tumor monoclonal antibody is C1 claim 1 , HAE3 claim 1 , or G1.3. The method of claim 1 , wherein determining the presence of the CSCs in the biological sample further includes using optical circuitry to detect the binding by identifying the specific binding of the glycan biomarker by the antibody ...

GLYCAN-BASED DRUGS, THERAPIES AND BIOMARKERS

The present disclosure discloses simple and efficient glycan- or carbohydrate-based processes or methods for the rapid identification of biological markers and therapeutic targets especially glycan-related targets of infectious diseases, cancers, autoimmune diseases, allergies, inflammation, toxicity, obesity and/or other disorders of humans, animals, plants and other organisms. Therefore, novel methods and products for the diagnosis, prevention, and treatment of such diseases obtainable based on these therapeutic targets can be developed. 2: The method of claim 1 , wherein the pharmaceutical composition is in the form of a tablet claim 1 , a capsule claim 1 , a pill claim 1 , a powder claim 1 , or granules.3: The method of claim 1 , wherein the pharmaceutical composition is administered orally.4: The method of claim 1 , wherein the analog of N-acetylneuraminic acid is N-acetylneuraminic acid methyl ester.5: The method of claim 1 , wherein the analog of N-acetylneuraminic acid is a hydroxylated analog of N-acetylneuraminic acid claim 1 , a glycoconjugate of N-acetylneuraminic acid or an N-acetylneuraminic acid containing an O- or N-glycosidic linkage to an amino acid.6: The method of claim 1 , wherein administration of N-acetylneuraminic acid methyl ester treats or prevents viral diarrhea in the patient.7: The method of claim 1 , wherein administration of N-acetylneuraminic acid methyl ester treats or prevents an infectious disease caused by an influenza virus claim 1 , a Newcastle disease virus claim 1 , or a rotavirus in the patient. This application is a divisional of U.S. application Ser. No. 14/803,725, filed Jul. 20, 2015, which is a divisional of U.S. application Ser. No. 12/900,913, filed Oct. 8, 2010, now U.S. Pat. No. 9,119,866, issued Sep. 1, 2015, which claims the benefit of priority from U.S. Provisional Application No. 61/278,685, filed Oct. 9, 2009, and U.S. Provisional Application No. 61/335,415, filed Jan. 7, 2010, and which is a continuation-in- ...

C-erbB-2 external domain: GP75

Disclosed are methods and compositions for identifying malignant tumors that overexpress the c-erbB-2 oncogene. Assays useful for diagnosis and prognosis of neoplastic disease are provided which detect the external domain of c-erbB-2, the glycoprotein gp75 and quantitate the level of gp75 in the biological fluids of mammals carrying a tumor burden. Further disclosed are recombinant, synthetically and otherwise biologically produced novel proteins and polypeptides which are encoded by the external domain DNA sequence of the c-erbB-2 oncogene (the gp75 gene) or fragments thereof. Such gp75 proteins and polypeptides are useful as vaccines, therapeutically in the treatment of cancer either alone or in combination with chemotherapeutic agents. Also disclosed are antibodies to such gp75 proteins and polypeptides which are useful diagnostically and therapeutically. Still further disclosed are test kits embodying the assays of this invention.

C-erbB-2 exrernal domain: gp75

Disclosed are methods and compositions for identifying malignant tumors that overexpress the c-erbB-2 oncogene. Assays useful for diagnosis and prognosis of neoplastic disease are provided which detect the external domain of c-erbB-2, the glycoprotein gp75 and quantitate the level of gp75 in the biological fluids of mammals carrying a tumor burden. Further disclosed are recombinant, synthetically and otherwise biologically produced novel proteins and polypeptides which are encoded by the external domain DNA sequence of the c-erbB-2 oncogene (the gp75 gene) or fragments thereof. Such gp75 proteins and polypeptides are useful as vaccines, therapeutically in the treatment of cancer either alone or in combination with chemotherapeutic agents. Also disclosed are antibodies to such gp75 proteins and polypeptides which are useful diagnostically and therapeutically. Still further disclosed are test kits embodying the assays of this invention.

非侵入性脑损伤诊断装置

本文提供一种在怀疑患有脑损伤的受试者中进行非侵入性诊断测试的非侵入性脑损伤诊断装置。用于诊断受试者的脑损伤的装置包括多孔基质的探测器，指示剂制剂，所述指示剂制剂设置在所述多孔基质上并且包含能够选择性结合指示样品中的脑损伤的基于聚糖的生物标志物的至少一种凝集素和/或抗体，以及视觉可检测标记；和与所述探测器连通的手柄，其中所述凝集素和/或抗体和/或所述视觉可检测标记中的至少一者被固定在所述多孔基质中的检测区中和/或所述检测区上，并且所述视觉可检测标记在所述基于聚糖的生物标志物与所述凝集素和/或抗体的结合事件后显示颜色强度水平并且变得可见。

C-erbB-2 foreign domain: GP75

ANTIBODIES, PHARMACEUTICAL COMPOSITIONS AND THEIR APPLICATIONS

РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) (13) 2016 138 744 A (51) МПК A61K 39/00 (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ЗАЯВКА НА ИЗОБРЕТЕНИЕ (21)(22) Заявка: 2016138744, 10.04.2015 (71) Заявитель(и): ОБИ ФАРМА ИНК. (TW) Приоритет(ы): (30) Конвенционный приоритет: 10.04.2014 US 61/977,824; 30.09.2014 US 62/057,381 (85) Дата начала рассмотрения заявки PCT на национальной фазе: 10.11.2016 US 2015/025305 (10.04.2015) (87) Публикация заявки PCT: A WO 2015/157629 (15.10.2015) Адрес для переписки: 119019, Москва, Гоголевский б-р, 11, этаж 3, "Гоулинг ВЛГ (Интернэшнл) Инк.", Карпенко Оксана Юрьевна R U (57) Формула изобретения 1. Антитело или его антигенсвязывающая часть, содержащие: первую определяющую комплементарность область тяжелой цепи (HCDR1), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 5 или SEQ ID NO: 31; вторую определяющую комплементарность область тяжелой цепи (HCDR2), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 6, SEQ ID NO: 24 или SEQ ID NO: 32; третью определяющую комплементарность область тяжелой цепи (HCDR3), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 7, SEQ ID NO: 25 или SEQ ID NO: 33; первую определяющую комплементарность область легкой цепи (LCDR1), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 8; вторую определяющую комплементарность область легкой цепи (LCDR2), характеризующуюся аминокислотной последовательностью приблизительно на 80% приблизительно на 100% гомологичную SEQ ID NO: 9 или SEQ ID NO: 35; и Стр.: 1 A 2 0 1 6 1 3 8 7 4 4 (54) АНТИТЕЛА, ФАРМАЦЕВТИЧЕСКИЕ КОМПОЗИЦИИ И ИХ ПРИМЕНЕНИЯ 2 0 1 6 1 3 8 7 4 4 (86) Заявка PCT: R U (43) Дата публикации заявки: 11.05.2018 Бюл. № 14 (72) Автор(ы): ЛАЙ Цзянн-Шиюнь (TW), ЧЭНЬ И- ...

Method for preparing sugar chains

【課題】標識効率に優れた糖鎖を調製する方法を提供する。【解決手段】本発明の糖鎖を調製する方法は、糖鎖を含有する糖鎖含有サンプルに標識試薬を加えることにより、糖鎖の標識体を含む標識生成物を得る標識工程を有する、糖鎖を調製する方法であって、標識工程において、標識試薬と糖鎖との反応環境中に水を含む、糖鎖を調製する方法。標識工程において、反応環境中の水の量をＸ（μＬ）、糖鎖の量をＹ（μｇ）としたとき、Ｘ／Ｙが、１．２以上である、糖鎖を調製する方法。【選択図】なし A method for preparing a sugar chain with excellent labeling efficiency is provided. The method for preparing a sugar chain of the present invention comprises a labeling step of obtaining a labeled product containing a labeled product of a sugar chain by adding a labeling reagent to a sugar chain-containing sample containing a sugar chain. A method for preparing a chain, wherein in the labeling step, water is included in the reaction environment of the labeling reagent and the sugar chain. In the labeling step, a method for preparing a sugar chain, wherein X / Y is 1.2 or more, where X (μL) is the amount of water in the reaction environment and Y (μg) is the amount of sugar chain. [Selection figure] None

Novel antibodies and methods of use for the treatment and diagnosis of cancer

The present invention is related to monoclonal antibodies, fragments, antigen binding portions or fragments thereof, for specific binding to human and/or mouse tumor associated carbohydrate antigens expressed on cancer cells, e.g., human colorectal adenocarcinma, non-small cell lung carcinoma (NSCLC). These antibodies can be used to induce selective cell death in cancer cells and for the treatment of cancer, e.g., NSCLC and/or in the diagnosis of cancers expressing tumor associated carbohydrate antigens in-vitro and in-vivo.

Glycan-interacting compounds

The present invention provides glycan-interacting antibodies useful in the treatment and prevention of human disease, including cancer. Such glycan-interacting antibodies include monoclonal antibodies, derivatives and fragments thereof as well as compositions and kits comprising them.

Means and methods for glycoprofiling of a protein

The present invention provides magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon including uses in methods for glycoprofiling of glycoproteins using lectins, e.g., in diagnostics of cancer. The magnetic carriers, anti-glycoprotein antibodies, the antigen binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein.

Biomarker for assessing pre-eclampsia

本文中公开了胎儿/母体健康筛选工具，例如用于评估先兆子痫的生物标志物。更具体地，公开了用于在对象中评估先兆子痫风险的方法，所述方法包括从所述对象获得第一血清样品、确定所述第一血清样品中糖基化纤连蛋白(GlyFn)的水平、以及将所确定的GlyFn水平与对照值进行比较，其中所确定的所述第一血清样品中的GlyFn水平相对于所述对照值的升高表明所述对象处于提高的先兆子痫风险中。还公开了在妊娠早期、妊娠中期或妊娠晚期确定对象中先兆子痫风险的方法、评估先兆子痫的严重程度和进展以及低出生体重或HELLP综合征之风险的并发症的方法。

Antibodies, pharmaceutical compositions and uses thereof

본 발명은 하나 이상의 탄수화물 항원에 결합하는 항체 또는 이의 항원-결합 부분을 제공한다. 또한 암 세포의 억제가 필요가 대상체에서 암 세포를 억제하기 위한 약학적 조성물 및 방법이 기재된다. 약학적 조성물은 항체 또는 이의 항원-결합 부분 및 적어도 하나의 약학적으로 허용되는 담체를 포함한다.

Neutralizing antibodies to ebola virus glycoprotein and their use

Antibodies and antigen binding fragments that specifically bind to ebolavirus glycoprotein and neutralize ebolavirus infection are disclosed. Nucleic acids encoding these antibodies, vectors, and host cells are also provided. The disclosed antibodies, antigen binding fragments, nucleic acids and vectors can be used, for example, to inhibit an ebolavirus infection in a subject.

Anti-cd27 antibody

Glycan arrays and method of use

The invention relates to linkers and methods for generating arrays with linkers. The invention also relates to methods for identifying agents that bind to various types of molecules on the arrays and to defining the structural elements of the molecules on the arrays that bind to those agents. The arrays and methods provided herein may be used for epitope identification, drug discovery and as analytical tools. The invention provides useful glycans and epitope determinants that are useful in detecting, diagnosing, recurrence monitoring and preventing cancer.

Method for measurement of glycoprotein, method for detection of hepatic diseases, reagent for quantification of glycoprotein, and sugar chain marker glycoprotein as measure of disease conditions of hepatic diseases

本发明提供一种能比过去更精准地检测肝病的糖链标志物糖蛋白的测定方法。本发明提供一种能比过去更精准地检测肝病的肝病检查方法。本发明提供一种用于上述测定方法的糖蛋白定量用试剂。本发明还提供一种能够根据肝病病情发展区别肝病病情的肝病病情指标糖链标志物糖蛋白。本发明提供的糖蛋白测定方法是对采自受检者的试样中所含α-1-酸性糖蛋白(AGP)和Mac-2-结合蛋白（M2BP）至少其中之一的糖蛋白进行测定，当糖蛋白为AGP时，测定与选自AOL和MAL的第一凝集素结合的AGP，当糖蛋白为M2BP时，测定与选自WFA、BPL、AAL、RCA120和TJA-II的第二凝集素结合的M2BP。

N-glycanes containing galactose-alpha-1,3-galactose in glycoprotein products produced from cho cells

FIELD: biotechnologies. SUBSTANCE: multiple populations of Chinese hamster ovary (CHO) cells undergo screening for ability to produce glycoproteins, which include glycans, containing terminal remains of galactose-alpha-1-3-galactose. The method of screening includes assessment of the level of glycans containing terminal remains of galactose-alpha-1-3-galactose, in multiple populations of Chinese hamster ovary (CHO) cells and selection of populations producing the specified glycans at the target level. Glycoprotein compositions produced by the Chinese hamster ovary (CHO) cells are analysed for availability of the specified glycans. The method of assessment of the glycoprotein composition includes measurement of the amount of terminal galactose-alpha-1-3-galactose. EFFECT: using the invention makes it possible to track and control content of terminal remains of galactose-alpha-1-3-galactose while using CHO cells as producers of therapeutic glycoprotein products. 28 cl, 11 dwg, 2 tbl, 1 ex РОССИЙСКАЯ ФЕДЕРАЦИЯ (19) RU (11) 2 484 142 (13) C2 (51) МПК C12Q C12Q C12N C12N 1/34 1/54 5/07 5/10 (2006.01) (2006.01) (2010.01) (2006.01) ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) ОПИСАНИЕ ИЗОБРЕТЕНИЯ К ПАТЕНТУ (21)(22) Заявка: 2011134491/10, 22.01.2009 (24) Дата начала отсчета срока действия патента: 22.01.2009 Приоритет(ы): (22) Дата подачи заявки: 22.01.2009 (45) Опубликовано: 10.06.2013 Бюл. № 16 C 2 2 4 8 4 1 4 2 R U C 2 (85) Дата начала рассмотрения заявки PCT на национальной фазе: 22.08.2011 (86) Заявка PCT: US 2009/031678 (22.01.2009) (87) Публикация заявки РСТ: WO 2010/085251 (29.07.2010) Адрес для переписки: 129090, Москва, ул.Б.Спасская, 25, стр.3, ООО "Юридическая фирма Городисский и Партнеры", пат.пов. А.В.Мицу, рег.№ 364 (54) СОДЕРЖАЩИЕ ГАЛАКТОЗА-АЛЬФА-1,3-ГАЛАКТОЗУ N-ГЛИКАНЫ В ГЛИКОПРОТЕИНОВЫХ ПРОДУКТАХ, ПОЛУЧЕННЫХ ИЗ КЛЕТОК СНО (57) Реферат: Изобретение относится к области биотехнологии и может быть использовано в фармацевтической промышленности. ...

Methods of identifying modulators of cellular glycosylation using gtrap3-18

The present invention provides methods and compositions for identifying compounds which modulate cellular glycosylation. The invention further provides methods for treating subjects suffering from or at risk of developing a glycosylation associated disorder.

Antibodies binding to tumour associated carbohydrate antigens, pharmaceutical compositions and uses thereof

The present invention provides antibodies or the antigen-binding portion thereof, that bind to one or more carbohydrate antigens. Also disclosed herein are pharmaceutical pharmaceutical compositions and methods for the inhibition of cancer cells in a subject in need thereof. The pharmaceutical compositions comprise an antibody or an antigen-binding portion thereof and at least one pharmaceutically acceptable carrier.

Methods, products and treatments for diabetes

The invention involves assays, diagnostics, kits, and assay components for determining levels of K41-glycated CD59 in subjects. Treatments for subjects based upon levels of K41-glycated CD59 also are provided.

Methods and reagents for the assessment of gestational diabetes

The invention involves assays, diagnostics, kits, and assay components for determining levels of glycated CD59 in the assessment of gestational diabetes mellitus and/or related disorders and/or conditions.

Saccharide-based biomarkers and therapeutics

The disclosure provides antibodies that specifically bind to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine, where the epitope is expressed by a cancer cell or an inflammatory intestinal cell. Also provided are compositions including these antibodies, as well as polynucleotides, vectors, host cells, and methods useful for production thereof. Further provided are methods an kits for treating or preventing cancer in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine, optionally in combination with another anti-cancer agent. Still further provided are methods and kits for treating or preventing gastrointestinal disease in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine. Yet further provided are methods and kits for detecting the presence of cancer cells in an individual including an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine.

Anti-cd27 antibody

Disclosed are: a monoclonal antibody which can specifically recognize CD27 containing a O-linked sugar chain having no galactose residue bound thereto and can bind to an extracellular domain of the CD27; and a method for utilizing the monoclonal antibody. Specifically disclosed are: a monoclonal antibody which can specifically recognize CD27 containing a O-linked sugar chain having no galactose residue bound thereto and can bind to an extracellular domain of the CD27, or a fragment of the antibody; a hybridoma capable of producing the antibody; DNA encoding the antibody; a vector carrying the DNA; a transformant produced by transforming with the vector; a method for producing an antibody or a fragment thereof by using the hybridoma or the transformant; and a diagnostic or therapeutic agent for a CD27-related disease, which comprises the antibody or a fragment thereof as an active ingredient.

Synthetic oligosaccharides for neisseria meningitis vaccine

The present invention provides synthetic oligosaccharides and conjugates thereof. The oligosaccharides may be synthesized by a chemical assembly methodology relying on a limited number of monosaccharide and disaccharide building blocks. The invention further provides immunogenic and immunoprotective compositions and antibodies derived therefrom for diagnosing, treating, and preventing infections caused by N. meningitidis.

Factor VII glycoforms

The present invention provides preparations of Factor VIIa polypeptides or Factor VIIa-related polypeptides that exhibit predetermined glycoform patterns. The preparations of the invention exhibit improved functional properties and are useful for treating Factor VII-mediated conditions.

Oligosialic acid derivatives, methods of manufacture, and immunological uses

The invention relates to methods of producing, and compositions comprising, an isolated alpha (2→8) or (2→9) oligosialic acid derivative bearing a non-reducing end enriched for one or more de-N-acetyl residues and resistant to degradation by exoneuraminidase. A representative production method involves: (i) treating an alpha (2→8) or (2→9) oligosialic acid precursor having a reducing end and a non-reducing end with sodium borohydride under conditions for de-N-acetylating the non-reducing end; and (ii) isolating alpha (2→8) or (2→9) oligosialic acid derivative having one or more de-N-acetylated residues and a non-reducing end that is resistant to degradation by exoneuraminidase. Isolated alpha (2→8) or (2→9) oligosialic acid derivatives that comprise a non-reducing end de-N-acetyl residue are provided, as well as antibodies specific for the derivatives, compositions comprising the derivatives, kits, and methods of use including protection against and detection of E. coli K1 and N. meningitidis bacterial infection, and in diagnosing and treating cancer.

Affinity matrix bearing tumor-associated antigens

Brassica gat event DP-073496-4 and compositions and methods for the identification and/or detection thereof

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

Brassica GAT event and compositions and methods for the identification and/or detection thereof

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

Brassica GAT event and compositions and methods for the identification and/or detection thereof

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

Methods of identifying modulators of cellular glycosylation using gtrap3-18

Biomarkers for assessment of preeclampsia

Novel monoclonal antibodies to lam and pim6/lam for diagnosing and treating infections caused by mycobacterium tuberculosis

FIELD: medicine; pharmaceuticals. SUBSTANCE: group of inventions refers to monoclonal antibodies directed to epitopes detected within lipoarabinomannan (LAM) for diagnosis and treatment of infections caused by Mycobacterium tuberculosis . Disclosed is a human monoclonal antibody to lipoarabinomannan (to LAM) or its antigen-binding portion, which specifically bind to LAM epitope, containing an Ara4 structure, an Ara6 structure or a combination thereof, wherein the LAM antibody comprises a light chain variable region CDR1 characterized by at least 80 % identity with SEQ ID NO: 1 or antigen fragments thereof, CDR2 of the light chain variable region, characterized by at least 80 % identity with SEQ ID NO: 2 or its antigen fragments, light chain variable region CDR3, characterized by at least 80 % identity with SEQ ID NO: 3 or SEQ ID NO: 26 or their antigen fragments, heavy chain variable region CDR1, characterized by at least 80 % identity with SEQ ID NO: 4 or its antigen fragments, heavy variable domain variable region CDR2, characterized by at least 80 % identity with SEQ ID NO: 5 or its antigen fragments, and CDR3 of heavy chain variable region, characterized by at least 80 % identity with SEQ ID NO: 6 or SEQ ID NO: 23 or their antigen fragments. Also disclosed is a kit for detecting at least one epitope of LAM, a method for diagnosing active tuberculosis infection in an individual and a method of treating tuberculosis infection in an individual. EFFECT: group of inventions provides effective treatment and diagnosis of tuberculosis infection. 15 cl, 32 dwg, 4 tbl, 2 ex РОССИЙСКАЯ ФЕДЕРАЦИЯ ФЕДЕРАЛЬНАЯ СЛУЖБА ПО ИНТЕЛЛЕКТУАЛЬНОЙ СОБСТВЕННОСТИ (12) (19) RU (11) (13) 2 732 502 C2 (51) МПК A61K 39/02 (2006.01) A61K 39/04 (2006.01) A61K 39/395 (2006.01) A61P 31/06 (2006.01) C07K 16/12 (2006.01) C07K 16/28 (2006.01) G01N 33/569 (2006.01) ОПИСАНИЕ ИЗОБРЕТЕНИЯ К ПАТЕНТУ (52) СПК A61K 39/02 (2020.02); A61K 39/04 (2020.02); A61K 39/395 (2020.02); A61P 31/06 (2020.02); C07K 16/ ...

Methods of identifying modulators of cellular glycosylation using GTRAP3-18

The present invention provides methods and compositions for identifying compounds which modulate cellular glycosylation. The invention further provides methods for treating subjects suffering from or at risk of developing a glycosylation associated disorder.

Advanced glycation end-product intermediaries and post-amadori inhibition

The instant invention provides compositions and methods for modeling post-Amadori AGE formation and the identification and characterization of effective inhibitors of post-Amadori AGE formation, and such identified inhibitor compositions.

Sugar biomarkers and therapeutic agents

Galactose-alpha-1, 3-galactose-containing n-glycans in glycoprotein products derived from cho cells

The present invention provides methods for evaluating a Chinese Hamster Ovary (CHO) cell population by measuring glycans containing terminal galactose-alpha-1-3-galactose residues produced by said cells, wherein the CHO cells have not been genetically engineered to express an alpha-galactosyl transferase coding sequence.

Method of diagnosing and stratifying anti-phospholipid syndrome

Disclosed are a method and reagents for diagnosis of anti phospholipid syndrome based on the levels of certain anti l can antibodies.

Methods and compositions for measuring natriuretic peptides and uses thereof

The present invention describes compositions and methods designed to determine the presence or amount of natriuretic peptides, or their fragments, in a sample. The degradation of natriuretic peptides is an ongoing process that may be a function of, inter alia, the elapsed time between onset of an event triggering natriuretic peptide release into the tissues and the time the sample is obtained or analyzed; the quantity of proteolytic enzymes present; etc. This degradation can produce circulating amounts of natriuretic peptides having reduced or lost biological function. The present invention provides, inter alia, assays designed to accurately measure biologically active natriuretic peptides, and compositions to inhibit a previously unknown pathway for degradation of natriuretic peptides.