Anti-Human MUC1 Recombinant Antibody (TAB-173) (CAT#: TAB-173)

Wu, Zhengliang L., et al. "Detecting substrate glycans of fucosyltransferases with fluorophore-conjugated fucose and methods for glycan electrophoresis." Glycobiology 30.12 (2020): 970-980. https://doi.org/10.1093/glycob/cwaa030

This study introduces a novel method for detecting substrate glycans of fucosyltransferases using fluorophore-conjugated fucose and gel electrophoresis techniques. The researchers demonstrated that various fucosyltransferases (FUT2, FUT6, FUT7, FUT8, and FUT9) can recognize and transfer fluorophore-conjugated fucose to their substrate glycans on glycoproteins. This approach allowed for the visualization and characterization of substrate glycans on fetal bovine fetuin, recombinant H1N1 viral neuraminidase, and therapeutic antibodies. The study established electrophoresis-based methods for analyzing free glycans, enabling the researchers to track the enzymatic synthesis of Lewis X and sialyl Lewis X structures. Importantly, the research revealed that fucosylation occurs at a much faster rate than sialylation, suggesting that fucosyltransferases are key regulatory targets in the synthesis of these important glycan epitopes.
Creative Biolabs provided Cantuzumab, an anti-Muc1 therapeutic antibody that lacks core-6 fucosylation. This antibody served as a critical test substrate for demonstrating FUT8's ability to incorporate fluorophore-conjugated fucose into substrate glycans, particularly for comparing glycan structures between antibodies with and without core fucosylation. The availability of this specialized therapeutic antibody enabled the researchers to clearly identify and characterize the substrate specificities of different fucosyltransferases, which has important implications for understanding glycan epitope regulation and potentially for developing targeted therapeutic interventions.