Endoglycosidase H (Endo H) is a recombinant glycosidase cloned from Streptomyces plicatus and overexpressed in E. coli. Endo H cleaves the chitobiose core of high mannose and a limited number of hybrid oligosaccharides from N-linked glycoproteins. It does not cleave complex glycans. Enzymatic cleavage is between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, leaving one N-acetylglucosamine residue on the asparagine. This is in contrast to PNGase F, which cleaves all asparagine-linked oligosaccharides. Protein Deglycosylation Mix is a mixture of five protein deglycosidases (PNGase F, O-Glycosidase, Neuraminidase, beta1-4 Galactosidase, beta-N-Acetylglucosaminidase) capable of removing glycans from both O-linked and N-linked glycosylation sites. Fetuin is provided as a deglycosylation substrate control. Fetuin is a glycoprotein with O-linked and N-linked glycosylation sites. PNGase F is a recombinant glycosidase cloned from Elizabethkingia miricola and overexpressed in E. coli. PNGase F has a molecular weight of 36kDa. For additional information about PNGase F, visit the PNGase F page.|