Application
Use N-glycosidase F to cleave all types of asparagine-bound N-glycans, provided that the amino group as well as the carboxyl group are present in a peptide linkage, and that the oligosaccharide has the minimum length of the chitobiose core unit. The reaction products are ammonia, aspartic acid (in the peptide chain), and the complete oligosaccharide.Note: N-Glycosidase F, recombinant is also available as a solution.
General description
N-Glycosidase F (PNGase F) is a potent enzyme which hydrolyzes at glycosylamine linkage. It also helps in generating a carbohydrate-free peptide and oligosaccharide with di-N-acetylchitobiose unit.
Peptide-N-glycosidase F, Peptide-N4-(acetyl-β-glucosaminyl)-asparagine amidase
Other Notes
For life science research only. Not for use in diagnostic procedures.
Physical form
Clear, colorless solution after reconstitution
Preparation Note
Storage conditions (working solution): 2 to 8 °CThe reconstituted solution is stable at 2 to 8 °C for at least four weeks.
Reconstitution
Dissolving the content in 0.1 ml redist water (100 unit package) or 0.25 ml double-dist. water (250 unit package) respectively, results in a concentration of 100 mM sodium phosphate buffer, 25 mM EDTA, pH 7.2.Note: N-Glycosidase F, recombinant is also available as solution with 50% glycerol.
Specificity
Hydrolyzes all types of N-glycan chains from glycopeptides and glycoproteins unless they carry α1,3-linked core fucose residues present in insect and plant glycoproteins. Free of contaminating proteolytic activities (x = H or sugar[s]) according to current quality control procedures.
Unit Definition
One unit is the enzyme activity which hydrolyzes 1 nmol dabsyl fibrin glycopeptide or 0.2 nmol dansyl fetuin glycoprotein within 1 minute at 37 °C and pH 7.8.
This product has met the following criteria: