Merck, P7367-300UN, PNGase F from Elizabethkingia meningoseptica

General description
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 stabilizers, 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.
Application
PNGase F from Elizabethkingia meningoseptica has been used:
for de-N-glycosylation of Zika20virus E protein
to evaluate coxsackievirus and adenovirus receptor glycosylation using CAR-expressing COS cells
to verify the N-linked glycosylation of MHC class 1 polypeptide-related sequence A (MICA)

Suitable for both proteomics and glycobiology use; compatible with MALDI-TOF MS analysis
Used to deglycosylate protein.
Biochem/physiol Actions
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
Other Notes
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.