Glycosidases

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 ...

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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, β1-4 Galactosidase, β-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.

Applications

• Determining the state of protein glycosylation.
• Characterizing glycan structure.

References

1. Maley, F. et al. (1989) Anal. Biochem. 180, 195–204.

References using Endo H to monitor protein trafficking:

1. Taner, S. et al. (2011) J. Immunol. 186, 62–72.
2. Beyer, S. et al. (2011) Endo. 152, 782–92.
3. Chen, Z. et al. (2011) J. Exper. Med. 208, 2633–40.
4. Iavarone, C. et al. (2011) J. Immunol. 186, 4213–22.
5. Guo, Y. et al. (2011) J. Exper. Med. 208, 2083–98.

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