Cleaves N-linked glycans from glycopeptides, including glycans with α(1,3)-linked core fucose as seen in insects and plants. Peptide N-Glycosidase A, Glycopeptidase from almonds, Almond glycoamidase, Peptide-N(4)-(N-acetyl-β glucosaminyl) asparagine amidase.
PNGase A from almonds cleaves N-Glycan chains linked to Asparagine from glycopeptides. The enzyme hydrolyzes an N(4)-(acetyl-β D-glucosaminyl) asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β D-glucosaminylamine and a peptide containing an aspartate residue.
The enzyme cleaves N-glycans with or without α(1,3)-linked core fucose residues present in insect and plant glycoproteins. This differs from PNGase F, which cannot remove N-glycans with α(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.
Ships with: WS0273 Reaction buffer: 50 mM citrate-phosphate buffer, pH 5.0, 0.02% sodium azide.
Lyophilized powder containing citrate-phosphate buffer, pH 5.0.
Optimum: pH 5.0 Range: pH 4.0 - 6.0
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.
Size: 10 mU
Product Code: GKE-5011B
1. Küster B, Wheeler SF, Hunter AP, Dwek RA, Harvey DJ. Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal Biochem. 1997 Jul 15;250(1):82-101.
2. Kolarich D, Altmann F. N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal Biochem. 2000 Oct 1;285(1):64-75.
Product Safety Documentation for GKE-5011B: