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.

The present disclosure provides materials and methods for identifying patients that are at risk of progression to clinically significant COVID-19 infection or disease.

Methods are provided for making rapid labeled dextran ladders and other calibrants useful in liquid chromatography. The methodologies include a two-step process comprising a reductive amination step of providing a reducing glycan and reacting it with a compound having a primary amine to produce an intermediate compound. The intermediate compound is then rapidly tagged with a rapid tagging reagent to produce the rapid labeled dextran ladder.

A method for measuring a glycated protein in a sample, the method comprising (1) a step of allowing a sample in which a degradation product has been generated from a glycated protein by a protease to react with an oxidoreductase in the presence of an electron mediator to generate a reduced electron mediator; and (2) a step of detecting the reaction state in the step (1) by an electrochemical technique using an interdigitated electrode.

The purpose of the present invention is to provide a novel monoclonal antibody having high affinity and that strictly recognizes, as a sugar chain epitope, only a “Siaα2,6Galβ1,4GlcNAc (6′-Sialyl-LacNAc): CDw75” sugar chain structure, being a molecular target for diagnosis of the malignancy of tumors. An anti-CDw75 monoclonal antibody is provided that recognizes “CDw75” sugar chain structures but does not recognize similar sugar chain structures indicated by “Galβ1,4GlcNAc”, “Siaα2,3Galβ1,4GlcNAc”, or “Siaα2,6Galβ1,4Glc”, by using a glycolipid antigen bonding a carrier lipid compound “HOCH.sub.2CH(NH—CO—(CH.sub.2).sub.22—CH.sub.3)—(CH.sub.2).sub.9—CH.sub.3 (C12L)” developed by the inventors to a “CDw75” sugar chain. The obtained anti-CDw75 monoclonal antibody is an excellent detection drug for B-cell lymphoma, gastric cancer, or colorectal cancer, an excellent diagnostic agent for tumor malignancy, etc., an excellent treatment agent for B-cell lymphoma, gastric cancer, or colorectal cancer, and an excellent prevention/treatment drug for influenza.

The methods disclosed herein include diagnosing a patient with MS, selecting a patient for further testing for MS, should the patient show elevated level of human IgG relative to an appropriate control. The methods also include differentiating subtypes of MS. The methods also include evaluating the efficacy of an MS drug or course of drug treatments, and/or treating MS. The methods include determining whether patients have elevated levels of IgG3-IgG1 immune complexes (which can include glycosylated IgG antibodies) in both blood and CSF. Methods also include diagnosing patients with primary-progressive MS (PPMS) and secondary-progressive MS (SPMS) where patients have higher levels of IgG3-IgG1 complexes in both CSF and blood, and reduced levels of albumin compared to patients with relapsing-remitting MS (RRMS). The methods optionally include treating the sample to dissociate immune and/or protein complexes, contacting the sample with a reagent that binds specifically to a human IgG or other protein, comparing the results to an appropriate control, and determining whether the patient has an altered level of IgG or other protein consistent with MS.

The present disclosure relates to a system for monitoring post-translational modification of protein using a biosensor with a gap, which performs with high reliability a diagnosis of a disease associated with a target protein for which impedance is measured, by measuring an impedance of a sample introduced into a sensor and calculating a change rate of the measured impedance, and to a method of manufacturing the biosensor used for the system.

Methods of analyzing glycosylated biomolecules include the steps of producing a deglycosylation mixture of biomolecules deglycosylated by natural or synthetic enzymatic or chemical techniques; providing a reagent solution having a labeling reagent in a polar aprotic, non-nucleophilic organic solvent; and mixing the deglycosylation mixture with the reagent solution in an excess of labeling reagent to produce derivatized glycosylamines. The method steps can be carried out purposefully without depletion of protein matter. A quenching solution can be added to the reaction mixture so that the pH of the reaction mixture is shifted to above 10. The yield of derivatized glycosylamines can be in an amount of about 80 to about 100 mole percent of the reaction mixture with minimal overlabeling, less than 0.2 mole percent. The derivizated glycosylamines can be separated from the reaction mixture and detected by chromatographic detection, fluorescence detection, mass spectrometry (“MS”), or Ultra Violet (“UV”) detection and/or a combination thereof.

The invention provides an analytical method for detecting bladder cancer by analysing a urine sample for presence of a glycan tumour antigen, the presence of which has been identified to indicate bladder cancer. The analytical method has the advantage that the tumour antigen can be analysed in a urine sample and has a high accuracy for indicating presence of cancer in the urinary tract, especially bladder cancer, e.g. the method has a low rate of false positive results.

The present disclosure an ELISA-based assay that uses a glycosylated polypeptide fragment derived from the SARS-CoV-2 spike protein (Covid-19) receptor binding domain (S1RBD) that has affinity for the extracellular domain of Angiotensin Converting Enzyme 2 (ACE2). The S1RBD polypeptide is generated by expression of an encoding nucleic acid by a human cell expression system resulting in glycosylation of the expressed spike receptor binding domain (S1RBD) protein at least at the N343 N-glycosylation site thereof, and which surprisingly and significantly increases the affinity of the S1RBD for ACE2, provides a significant increase in the sensitivity of the assay compared to other known assays.