Glyko® sequencing-grade Endo H
[endo-beta-Nacetylglucosaminidase H, EC 3.2.1.96] is isolated from a strain of E. coli expressing a cloned gene from Streptomyces plicatus.
Ships w/ Incubation Buffer & Denaturation Solution.
Applications:
- Release of asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycopeptides and glycoproteins
- Cell biology/protein intracellular trafficking studies
- Therapeutic recombinant protein analysis
- Glycan studies of therapeutic antibodies and process development changes
- AIDS/HIV research
- Functional role of glycans on proteins
Specificity:
Asparagine-linked hybrid or high-mannose oligosaccharides, either as free glycopeptides or as protein-linked glycans, are substrates for the enzyme. However, the enzyme does not cleave complex type glycans. Thus, Endo H is an extremely useful tool for delineating between these two types of N-linked structures on proteins.
In many cases, glycan removal with Endo H results in a significant reduction in apparent molecular weight of the protein substrate, leading to a detectable change in its electrophoretic migration when evalluated with SDS-PAGE.
The enzyme is also active against dolichollinked glycans containing these structures.
The presence of sulfate on oligomannose glycans may impair or reduce the rate of
enzyme cleavage.
Further information:
GKE-5002 Endo H Tech Sheet 031606AA.pdf
Tech Info: [Endo-ß-N-acetylglucosaminidase H] cleaves between the N-acetylglucosamine residues of the chitobiose core of N-linked glycans. Will cleave oligomannose and most hybrid-type glycans, including those which are core fucosylated, whereas complex-type glycans are not hydrolyzed.
insert specs
Ships w/ Incubation Buffer & Denaturation Solution