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.
- Do detergents inhibit exoglycosidases/endoglycosidases?
- What are glycosidases and their uses?
- Can glycosidases be used in combination for extensive digestion?
- Can glycosidases be used on whole cells?
- Could exoglycosidases change the migration of my protein?
- How are exoglycosidases removed from a reaction?
- How specific are NEB exoglycosidases?
- Endo-α-N-Acetylgalactosaminidase Application Note 1
- Protocol for α1-3,6 Galactosidase (P0731)
- Typical Reaction Conditions for α2-3,6,8 Neuraminidase (P0720)
- Typical Reaction Conditions for α1-2 Fucosidase (P0724)
- Typical Reaction Conditions for β-N-Acetylhexosaminidasef (P0721)
- Typical Reaction Conditions for β1-3 Galactosidase (P0726)
- Typical Reaction Conditions for α1-6 Mannosidase (P0727)
- Typical Reaction Conditions for α1-2,3 Mannosidase (P0729)
- Typical Reaction Conditions for α1-3,6 Galactosidase (P0731)
- Typical Reaction Conditions α-N-Acetylgalactosaminidase (P0734)
- Typical Reaction Conditions for β1-4 Galactosidase S (P0745)
- Typical Reaction Conditions for α2-3,6,8,9 Neuraminidase A (P0722)
- Typical Reaction Conditions for α2-3 Neuraminidase S (P0743)
- Typical Reaction Conditions for β-N-Acetylglucosaminidase S (P0744)
- Typical Reaction Conditions for α1-3, 4, 6 Galactosidase (P0747)
- Typical Reaction Conditions for α1-2, 3, 4, 6 Fucosidase (P0748)
- Typical Reaction Conditions for α1-3, 4 Fucosidase (P0769)
- Typical Reaction Conditions for β1-3,4 Galactosidase Reaction Protocol (P0746)
- Reaction Protocols for Protein Deglycosylation Mix II (P6044)
- Typical Reaction Conditions for a1-2,3,6 Mannosidase (P0768)
- a1-2,4,6 Fucosidase O Digestion of Released Labeled Glycans Protocol
The Structure, Function and Importance of Carbohydrates
Read about the structure, function, and importance of Carbohydrates from biology experts at NEB.
- Glycoproteomics Brochure
- Detailed Characterization of Several Glycosidase Enzymes
- Glycobiology Unit Conversion Chart
- Vainauskas, S., Kirk, C.H., Petralia, L., Guthrie, E.P., McLeod, E., Bielik, A., Luebbers, A., Foster, J.M., Hokke, C.H., Rudd, P.M., Shi, X., Taron, C.H 2018. A novel broad specificity fucosidase capable of core a1-6 fucose release from N-glycans labeled with urea-linked fluorescent dyes Sci Rep. , PubMedID: 29934601, DOI: 1038/s41598-018-27797-0
- O'Flaherty, Roisin, Harbison, Aoife M., Hanley, Philip J., Fadda, Elisa, Rudd, Pauline, Taron, Chris 2017. Aminoquinoline fluorescent labels obstruct efficient removal of N-glycan corex Journal of Proteome Research. 16, PubMedID: , DOI:
- Albrecht, S., Vainauskas, S., Stöckmann, H., McManus, C., Taron, C.H. and Rudd, P.M. 2016. Comprehensive Profiling of Glycosphingolipid Glycans Using a Novel Broad Specificity Endoglycoceramidase in a High-Throughput Workflow. . May 3;88(9), PubMedID: 27033327, DOI:
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Learn about the core sequences and common modifications of N-linked and O-linked glycans in this video. Analysis of these glycans can be accomplished with the use of deglycosylation enzymes, which can provide complete sugar removal with no protein degradation.
Learn how glycosidases are used to analyze multiple glycoprotein samples. Here, the model glycoprotein, hCGβ, which carries both N- and O-glycans, is demonstrated.