Description
In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides.
Abbr
PNGase F, Recombinant (Flavobacterium meningosepticum)
Species
Flavobacterium meningosepticum
Product Overview
PNGase F, peptide N-glycosidase F, is a recombinantly expressed endoglycosidase from Flavobacterium meningosepticum that cleaves the β-aspartylglucosamine bond between the N-Acetylglucosamine (GlcNAc) and asparagine linkage of N-linked oligosaccharides in glycoproteins. This cleavage point acts as a convenient identification point in subsequent mass spectroscopy analysis.
Form
20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA
Molecular Weight
34,800 daltons (Apparent)
Unit Definition
One unit is defined as the amount of enzyme required to catalyze the release of >95% N-linked oligosaccharides from 60 μmoles of denatured ribonuclease B in 1 hour at 37C, pH 7.5. One micromolar unit of PNGase F activity is equal to 1,000 nanomolar units (IUB milliunits).
Storage
2-8°C. Avoid multiple freeze/thaw cycles.
Synonyms
glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8
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