PNGase F, peptide Nglycosidase F from Flavobacterium meningosepticum, catalyzes the hydrolysis of asparaginelinked high mannose, as well as hybrid and complex oligosaccharides from glycoproteins (1). Unlike glycosidases that hydrolyze glycosidic bonds, PNGase F is an amidase that cleaves the betaaspartylglucosamine bond between the innermost GlcNAc of Nglycans and asparagine residues of glycoproteins (2). The enzyme is highly active on various Nglycans except those with the innermost GlcNAc modified with alpha13linked core fucose, which is commonly found on plant Glycoproteins (3). Cleavage with PNGase F will convert the asparagine residue to an aspartic residue, allowing identification of the glycosylation sites by mass spectrometry (4). Recombinant PNGase F’ is a fusion of human cystatin A to PNGase F. PNGase F’ is a good alternative for PNGase F for deglycosylating proteins that have similar mass to PNGase F.
Source:Recombinant protein corresponding to aa41-354 from F. meningosepticum PNGase F', fused to 6-his tag at C-terminal, NS0-derived.
Molecular Weight:~44-48kD
Biological Activity:Measured by its ability to deglycosylate ribonuclease B under denatured conditions. >50% ribonuclease B (10ug) is deglycosylated by 30ng of Recombinant F. meningosepticum PNGase F' within 30 minutes, as measured under the described conditions.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：20ug
Source Antigen：Recombinant, E. coli
Grade：Purified
Purity：~90% (SDS-PAGE)
Form：Supplied as a liquid in Tris, NaCl, EDTA. BSA free.
