AdvanceBio PNGase A (almond), 2 mU

SKU: GKE-5020B-1 Categories: ,


  • Enzyme cleaves N-linked glycans from glycopeptides, including glycans with α(1,3)-linked core fucose as seen in insects and plants.
  • Incudes reaction buffer:
    • 50 mM citrate-phosphate buffer,
    • pH 5.0, 0.02% sodium azide.


  • Enzyme Specific Activity : 5 units/mg
  • pH Range : 4-6
  • Enzyme Specificity
    • PNGase A from almonds cleaves N-glycan chains linked to Asparagine from glycopeptides.
    • The enzyme hydrolyzes an N(4)-(acetyl-ß D-glucosaminyl) asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-ß D-glucosaminylamine and a peptide containing an aspartate residue.
    • The enzyme cleaves N-glycans with or without a(1,3)-linked core fucose residues present in insect and plant glycoproteins.
    • This differs from PNGase F, which cannot remove N-glycans with a(1,3)-linked core fucose. PNGase A requires glycopeptides as substrates.
    • Glycopeptides can be obtained by digesting the glycoprotein with trypsin [1,2] or pepsin.
    • Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino acid residues in the substrate.
  • Enzyme Unit Definition : One unit is defined as the amount of enzyme required to hydrolyze 1 µmol ovalbumin glycopeptide per min at pH 5.0 and 37°C
  • Enzyme Formulation : Lyophilized powder containing citrate-phosphate buffer, pH 5.0.
  • Enzyme Source : Almond. Enzyme also knows as Peptide N-Glycosidase A, Glycopeptidase from almonds, Almond glycoamidase, Peptide-N(4)-(N-acetyl-β glucosaminyl) asparagine amidase.
  • Unit : 2 mU
  • Molecular Weight : 54.2 and 21.2 kDa
  • pH Optimum : 5

*Available in different unit and packing size

GKE-5011A, 2mU

GKE-5011B, 10mU



AdvanceBio PNGase A (almond), 2 mU