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PNGase F, Chryseobacterium, native. Native PNGase F (formerly ProZyme), peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Also available as a recombinant product, AdvanceBio N-Glycanse, see GKE-5006A. Includes 5x reaction buffer, denaturation solution, detergent solution

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  • 50 µL
  • Structural analysis of O-glycan
Enzyme Specificity
  • PNGase F releases intact N-linked oligosaccharides from glycoproteins and glycopeptides. The enzyme will not cleave oligosaccharides from a single asparagine residue and cleavage does not occur if there is core α1-3 linked fucose as commonly encountered in plant glycoproteins Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage.
Enzyme Applications
  • PNGaseF is used to release intact N-linked glycans from glycopeptides and glycoproteins
  • structure-function studies of N-glycosylated glycoproteins
  • preparation of deglycosylated proteins for molecular weight estimation or crystallography studies
Enzyme Unit Definition
  • One unit of N-Glycanase is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 μmole of denatured ribonuclease B per minute at pH 7.5 and 37°C
Enzyme Formulation
  • 52 mM Tris-HCl, 36 mM NaCl, 9 mM sodium acetate, 5 mM EDTA, 0.02% sodium azide (pH 7.5), glycerol-free formulation
Enzyme Source
  • Native, purified from Elizabethkingia meningoseptica. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum 
  • ≥2 U/mL
  • 100 mU
pH Optimum
  • 7.5