PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation

• of recombinant soybean agglutinin (rSBA) in Nicotiana benthamiana (NbrSBA) and Solanum tuberosum (StrSBA)
• of frontal cortical lysate to verify the glycosylation profile of β-secretase (BACE proteins)
• of cell lysate for evaluating the siRNA silencing of cellular prion protein (PrP^c) post transfection

PNGase F is a glycosylasparaginase used to deglycosylate proteins. It is widely used in structure-function studies of glycoproteins.

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.

PNGase F cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain. It deaminates the asparagine to aspartic acid, but leaves the oligosaccharide intact. PNGase F will not remove oligosaccharides containing α(1-3)-linked core fucose, commonly found in plant glycoproteins. A tripeptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F.

Each set includes enzyme, two formulations of 5× reaction buffer (for routine and mass spectrometry downstream analysis), detergent and denaturation solutions

One unit will catalyze the release of N-linked oligosaccharides from 1 micromole 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.

N-Glycanase is a registered trademark of Agilent Technologies Inc