NEB offers a wide selection of exoglycosidases for glycobiology research. Exoglycosidases are glycoside hydrolase enzymes that cleave the glycosidic linkage of a terminal monosaccharide in an oligosaccharide or polysaccharide. Because each residue is removed separately, a series of exoglycosidases, each one cleaving at a specific glycolic linkage, is needed. These exoglycosidases can be used to remove a terminal sugar residue, to determine the sequence of a glycan, or for modifying glycans on glycoproteins.

Many of these reagents are recombinant, and all undergo several quality control assays, enabling us to provide products with lower unit cost, high purity, and reduced lot-to-lot variation. All of our glycosidases are tested for contaminants. Since p-nitrophenyl-glycosides are not hydrolyzed by some exoglycosidases, we use only flourescently-labeled oligosaccharides to assay activity and screen for contaminating glycosidases.

  1. Overview of Glycobiology

    Learn about the core sequences and common modifications of N-linked and O-linked glycans in this video. Analysis of these glycans and/or peptide portions of the glycoprotein can be accomplished with the use of deglycosylation enzymes, which are explained in detail. Unlike other chemical deglycosylation methods, enzymatic treatment is much gentler and can provide complete sugar removal with no protein degradation.

  2. Identification and Characterization of Protein Glycosylation P6039S

    Here we illustrate the use of glycosidases for the analysis of a model glycoprotein: recombinant human chorionic gonadotropin beta (hCGβ), which carries both N-glycans and O-glycans in this video. The technique requires only simple instrumentation and typical consumables, and it can be readily adapted to the analysis of multiple glycoprotein samples.