Endoglycosidase F3 [For Glycan Release] (CAT#: CB-P254-K) Datasheet

Kit

Selectively release triantennarry and fucosylated biantennary N-glycans N-glycans from peptides and proteins.
Endo F3 cleaves free or asparagine-linked tritactose or α(1-6) fucosylated bicontact oligosaccharides, as well as the core structure of tricarbamylchitobiose. Non-fucosylated biantennary glycans will also be cleaved, but the decomposition 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 in which one N-acetylglucosamine residue remains in the asparagine on. In contrast, PNGase F completely removes oligosaccharides. Alpha (1-3) fucosylation will inhibit enzyme activity. It has no activity on oligomannose and hybrid molecules.

Source: Recombinant Elizabethkingia miricola in E. Coli
EC: 3.2.1.96
Alternative Names: Endo F3, Endoglycosidase F3, endo-β-N-acetylglucosaminidase F
Specific Activity:
Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of porcine fibrinogen in 1 minute at 37°C, pH 4.5. Cleavage is monitored by SDS-PAGE (cleaved fibrinogen migrates faster).
Purity: Endoglycosidase F3 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.
Specificity:Cleaves all asparagine-linked triantennary or α(1-6) fucosylated biantennary oligosaccharides, as well as triamannosyl chitobiose core structures. α(1-3) fucosylation will inhibit enzymatic activity. Nonfucosylated biantennary glycans will also be cleaved, but at a 40x reduced rate. (Note: The recombinant version is not glycosylated, which may result in properties differing from the native protein.)
Specific Activity:>25 U/mg
Activity:>5 U/mL
Molecular weight: 30,000 daltons