- Unit of Measure:
- EA
- pH Range:
- 7.5-9.5
- Volume:
- 400 uL
- Concentration:
- 2.5 U/mL
- Enzyme Applications:
- Release of intact N-linked glycans from glycopeptides and glycoproteins;Structure-function studies of N-glycosylated glycoproteins;Preparation of deglycosylated proteins for molecular weight estimation or crystallography studies
- Enzyme Formulation:
- 20 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA (pH 7.5)
- Enzyme Source:
- Recombinant gene from Elizabethkingia meningoseptica, expressed in E
- coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum. Enzyme is also known as peptide-N-glycosidase F, peptide-N4-(N-acetyl- Beta -glucosaminyl)asparagine amidase. Enzyme Specific Activity:
- >= 10 units/mg
- Enzyme Specificity:
- Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless a(1-3) core fucosylated, as in plant glycans and some insect glycans
- Asparagine must be peptide bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free. Enzyme Unit Definition:
- One unit is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 umole of denatured ribonuclease B per minute at 37 C, pH 7.5
- MolecularWeight:
- ~35,000 daltons
- pH Optimum:
- 8.6
- Units Of Product:
- 1 U
