Product Description Endo F1, Endoglycosidase F1, endo-beta-N-acetylglucosaminidase F Endo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endo F1 Specifictity Cleaves all asparagine-linked high mannose and some hybrid oligosaccharides
Source recombinant Elizabethkingia miricola (was Chryseobacterium meningosepticum) in E. Coli
EC 3.2.1.96 Specific Activity >16 U/mg Activity >17 U/ml Molecular weight 32,000 daltons
Specific Activity Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured Ribonuclease B (RNase B) in 1 minute at 37˚C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved RNase B migrates faster).
Contents 60 µl aliquot of enzyme (1 U) in 20 mM Tris-HCl, pH 7.5
Included with 20 µL and 60 µL pack sizes: 5x Reaction Buffer – 250 mM sodium phosphate, pH 5.5
Suggested usage 1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water. 2. Add 10 µl 5x Reaction Buffer 5.5 3. Add 2.0 µl of Endo F1. Incubate 1 hour at 37ˆC.
Storage
Store enzyme at 4˚C. Stability Stable at least 12 months when stored properly. Several days exposure to ambient tempertures will not reduce activity. Purity Endoglycosidase F1 is tested for contaminating protease as follows; 10 μg of denatured BSA is incubated for 24 hours at 37oC with 2 μL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.
The production host strain has been extensively tested and does not produce any detectable glycosidases. | 
