Glycopeptidase F
PNGase F

Liquid. In 50 mM NaCl, 20 mM Tris-HCl, 1 mM EDTA, pH 7.5. DO NOT FREEZE. Native N-Glycosidase F from Elizabethkingia meningosepticum. Catalyzes the hydrolysis of asparagine-linked high mannose, as well as hybrid and complex oligosaccharides from glycoproteins. This enzyme will not cleave oligosaccharides containing a1,3-linked core fucose commonly found on plant glycoproteins. N-Glycosidase F will also fail to cleave if the asparagine to which the oligosaccharide is attached is not peptide-bonded to at least one amino acid residue at both the amino and carboxy termini. Activity: ≥4500 units/ml. Specific activity: ≥20,000 units/mg protein. One unit is defined as the amount of enzyme that will catalyze the release of N-linked oligosaccharides from 1.0 nmol denatured ribonuclease B per min at 37°C, pH 7.5. Cleavage is monitored by SDS-PAGE. One unit of N-Glycosidase F is equal to 1 IUB milliunit. Contaminants: Proteases: none detected.. EC 3.5.1.52, CAS 83534-39-8.

Ref.: Means, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181. Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058. Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44. Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.