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.
- How specific are NEB exoglycosidases?
- How are exoglycosidases removed from a reaction?
- Could exoglycosidases change the migration of my protein?
- Do detergents inhibit exoglycosidases/endoglycosidases?
- Can glycosidases be used on whole cells?
- What are glycosidases and their uses?
- Can glycosidases be used in combination for extensive digestion?
- Typical Reaction Conditions for α1-3,6 Galactosidase (P0731)
- Typical Reaction Conditions for α1-2,3 Mannosidase (P0729)
- Typical Reaction Conditions for β-N-Acetylhexosaminidasef (P0721)
- Typical Reaction Conditions for α1-6 Mannosidase (P0727)
- Typical Reaction Conditions for β1-3 Galactosidase (P0726)
- Typical Reaction Conditions for β1-4 Galactosidase S (P0745)
- Typical Reaction Conditions for α2-3 Neuraminidase S (P0743)
- Typical Reaction Conditions for β1-3,4 Galactosidase Reaction Protocol (P0746)
- Typical Reaction Conditions for α1-2 Fucosidase (P0724)
- Protocol for α1-3,6 Galactosidase (P0731)
- Typical Reaction Conditions α-N-Acetylgalactosaminidase (P0734)
- Typical Reaction Conditions for α2-3,6,8,9 Neuraminidase A (P0722)
- Typical Reaction Conditions for β-N-Acetylglucosaminidase S (P0744)
- Typical Reaction Conditions for α1-3, 4 Fucosidase (P0769)
- 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 a1-2,3,6 Mannosidase (P0768)
- a1-2,4,6 Fucosidase O Digestion of Released Labeled Glycans Protocol
- Typical Reaction Conditions for α2-3,6,8 Neuraminidase (P0720)
- Reaction Protocols for Protein Deglycosylation Mix II (P6044)
- Endo-α-N-Acetylgalactosaminidase Application Note 1
N-Glycan Composition Profiling for Quality Testing of Biotherapeutics
The Structure, Function and Importance of Carbohydrates
Read about the structure, function, and importance of Carbohydrates from biology experts at NEB.
The Glycobiology brochure provides information on the suite of endo- and exoglycosidases, and deglycosylation enzymes offered by NEB.
The Glycoproteomics brochure provides information on the suite of endo- and exoglycosidases, and deglycosylation enzymes offered by NEB.
- Detailed Characterization of Several Glycosidase Enzymes
- Glycobiology Unit Conversion Chart
While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.
For more information about commercial rights, please contact NEB's Global Business Development team at [email protected].
This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
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.