Endoglycosidase H [For Glycan Release] (CAT#: CB-P255-K) Datasheet

Kit

Endo H cleaves asparagine-linked hybrid or high mannose oligosaccharides, but does not cleave complex oligosaccharides.
Endo H cleaves asparagine-linked hybrid or high mannose oligosaccharides, but does not cleave complex oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetyl chitobiose core of the oligosaccharide to produce a truncated sugar molecule in which one N-acetylglucosamine residue remains in the asparagine on. In contrast, PNGase F completely removes oligosaccharides. Detergents and heat denaturation can increase the cleavage rate of certain glycoproteins.

Source: recombinant from Streptomyces plicatus in E.Coli
EC: 3.2.1.96
Alternative Names: Endo H, endo-β-N-acetylglucosaminidase H, Endoglycosidase H
Specific Activity: One unit of Endo H activity is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 µmole of denatured Ribonuclease B. Cleavage is monitored by SDS-PAGE (cleaved Ribonuclease B migrates faster).
Specific Activity:>40 U/mg
Activity:>5 U/mL

Molecular weight: 29,000 daltons
pH range: 5-6, optimum 5.5
Purity: Endoglycosidase H is tested for contaminating protease as follows; 10 µg of denatured BSA is incubated for 24 hours at 37°C with 2 µL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.