PNGase F from Elizabethkingia meningoseptica 

Used to deglycosylate protein.

Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.

One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit.

Proteomics Grade PNGase F has been extensively purified and lyophilized from dilute potassium phosphate buffer to produce a stable product. The product is free from glycerol and other stablizers, and contains very low levels of buffer salts. This highly purified material is excellent for N-linked deglycosylation of glycoproteins or glycopeptides in gel, in solution, or on blot membranes.

Proteomics Grade

≥95% (SDS-PAGE)

≥1 yr at 2-8 °C, (Solution is stable for at least 3 freeze-thaw cycles), ≥1 weeks at 2-8 °C (for a reconstituted solution >500 units/ml)

mol wt ~36 kDa

~6.8

wet ice

2-8°C

Plummer, T.H., et al. J. Biol. Chem. 259, 10700, (1984)

Tarentino, A.L., et al. Biochemistry 24, 4665, (1985)

2

PP0201, Glycoprofile^™ II, Enzymatic In-Solution N-Deglycosylation Kit

PP0200, GlycoProfile^™ I, In-Gel Deglycosylation Kit