N-GLYCOSIDASE F LYO. 250 U

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.

N-glycosidase F, also known as PNGase F, is an asparagine amidase enzyme derived from Flavobacterium meningosepticum. It is widely used as a valuable tool in protein research to investigate and analyze N-glycosylation.

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.

Application

N-Glycosidase F has been used for deglycosylation of N-glycoproteins.

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.

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.

Physical form

Clear, colorless solution after reconstitution

Preparation Note

Storage conditions (working solution): 2 to 8 °C
The 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.

Other Notes

For life science research only. Not for use in diagnostic procedures.