Native PNGase F (Peptide N Glycosidase F), 1 U / 200 µL [For Glycan Release] (CAT#: CB-P250-K) Datasheet

Kit

PNGase F is suitable for releasing all types (high mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGaseF does not remove the α(1-3) linkages commonly found on plant glycoproteins The core fucose is an oligosaccharide.
PNGase F cleaves N-linked (asparagine linked) oligosaccharides from glycoproteins. The enzyme deaminates asparagine to aspartic acid, leaving oligosaccharides intact. Denaturation increases the cutting rate. Most natural proteins can still be completely N-deglycosylated, but the incubation time must be increased. The enzyme will remain fully active for at least 96 hours under the reaction conditions (37°C). PNGase F does not remove oligosaccharides containing Alpha-(1,3)-linked core fucose, which are commonly found on plant glycoproteins; for this, please use peptide N-glycosidase A.

There are many alternative enzymes that can be used to remove N-glycans, especially Endo F enzyme and EndoH. These enzymes cleave between the two N-acetylglucosamine residues in the oligosaccharide core, resulting in a truncated sugar molecule with an N-acetylglucosamine residue remaining on asparagine. This leaves the charged sugars, which can help keep the protein in the solution, which will precipitate after deglycosylation with PNGase F, thereby completely removing the oligosaccharides. Endo F1 cracks high mannose and some hybrid N-glycans. Endo F2 will eliminate dual antennas and high mannose (reduce the rate by 40 times). Endo F3 release of endotriol and fucosylated biantennary N-glycans. Endo H removes heterozygous or high mannose glycans.

Contents: PNGase F in 20 mM Tris-HCl, pH 7.5 - 200µL
Specific Activity:>25 U/mg
Activity: 5 U/mL
Molecular weight: 36,000 daltons
pH range: 6-10, optimum 7.5
Source: Elizabethkingia miricola (was Chryseobacterium meningosepticum)