Endoglycosidase F2 [For Glycan Release] (CAT#: CB-P253-K) Datasheet

Kit

Selective release of biantennary and high mannose (40-fold reduction) glycans from peptides and proteins.
Endo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It can also cut high mannose glycans, but the cutting rate is reduced by 40 times. It cleaves between the two N-acetylglucosamine residues in the diacetyl chitobiose core of the oligosaccharide to produce a truncated sugar molecule, one of which remains in the asparagus Amide on. In contrast, PNGase F completely removes oligosaccharides.
Endoglycosidase F2 is less sensitive to protein conformation than PNGase F, so it is more suitable for natural protein deglycosylation. However, for best results, denaturation of glycoproteins is recommended.

Source: Recombinant Elizabethkingia miricola in E. Coli
EC: 3.2.1.96
Alternative Names: Endo F2, Endoglycosidase F2, endo-β-N-acetylglucosaminidase F2
Specificity:Cleaves all asparagine-linked biantennary oligosaccharides and high mannose (though at a 40X reduced rate) N-glycans from peptides and proteins
Specific Activity:>20 U/mg
Activity:>5 U/mL
Molecular weight: 32,000 daltons
Purity: Endoglycosidase F2 is tested for contaminating protease as follows; 10 µg of denatured BSA is incubated for 24 hours at 37°C with 2 µL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.