Description
| Application: | Removal of N-linked high mannose oligosaccharides from glycoproteins by SDS-PAGE gel shift assay. For research use only! |
| Identity: | Streptomyces plicatus enzyme, recombinant from E. coli |
| Unit defintion: | One unit is defined as the amount of enzyme required to remove > 95 % of the carbohydrate from 10 μg of denatured RNase B in 1 hour at 37 °C in a total reaction volume of 10 μl. |
| Size: | 271 amino acids; MWcalc. = 29.0 kDa |
| Purity: | > 95 % by SDS-PAGE |
| Buffer composition: | Frozen liquid, 50 mM NaCl, 20 mM Tris-HCl, 5 mM EDTA, pH 7.5 (@ 25 °C) |
| Storage: | store at -20 °C |
| Expression system: | E. coli |
| Composition: | Animal component free |
Endoglycosidase H (Endo H) is a recombinant glycosidase that has been cloned from Streptomyces plicatus and overexpressed in E. coli. It has been established that Endo H is capable of cleaving the chitobiose core of high mannose and a limited number of hybrid oligosaccharides from N-linked glycoproteins. It has been demonstrated that the enzyme does not cleave complex glycans. Enzymatic cleavage occurs between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, resulting in the retention of one N-acetylglucosamine residue on the asparagine. This is in contrast to PNGase F, which cleaves all asparagine-linked oligosaccharides.
If you need any more information at all, or if you’ve cited our amazing recombinant Endo H in a publication, please don’t hesitate to get in touch! We would absolutely love to hear from you and would be thrilled to reward your research.
