PNGase F (CystatinA Tag), Recombinant, F. meningosepticum, aa41-354

Blue Ice

4448

Supplied as a liquid in Tris, NaCl, EDTA. BSA free.

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.

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.