AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL. A recombinant form of PNGase F, releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Does not include reaction buffers that ship with 'A' (100 mU) and 'B' (200 mU) pack sizes. Please contact us if you require buffers. Supplied at a concentration of ≥ 2.5 U/mL. For a more concentrated formulation of ≥ 10 U/mL, which may be useful for native digestions, see GKE-5010B or GKE-5020B (EDTA-free).
- 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
