Removal of Fc N-glycans abolishes ADCC activity, enabling direct study of glycan-mediated Fc receptor interactions and antibody function.
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Selective enrichment of IgA O-glycopeptides for improved detection and characterization of hinge-region glycosylation.
Selective enrichment of O-glycoproteins from human serum for improved LC-MS/MS detection and glycosylation-focused proteomic analysis.
O-glycan site occupancy profiling and complete deglycosylation of etanercept for in-depth characterization of complex O-glycoproteins.
Confirmation and quantification of Tn antigens on O-glycosylated biopharmaceuticals while simplifying intact-mass analysis and revealing protein variants.
Removal of glycan β-galactose to simplify IgG glycan heterogeneity, improve LC-MS analysis, and reveal underlying glycation modifications.
Functional comparison of antibody glycoforms by combining glycoengineering with ADCC and ADCP reporter assays to assess Fc effector activity.
Higher-resolution flow cytometry with improved signal intensity and a 10-fold increase in separation index using site-specific antibody labeling.
Supports high-quality immunofluorescence imaging with consistent signal intensity and reliable quantification through defined antibody labeling.
Improved PET/CT tumor targeting and biodistribution using site-specific antibody labeling with consistent DOL and preserved in vivo performance.
Site-specific ADC generation with defined DAR, preserving antigen binding and delivering potent, controlled cytotoxicity in target cells.
Arginine-specific peptide mapping with improved perfomance over Arg-C, generates larger peptides complementary to trypsin.
