AdvanceBio N-Glycanase (PNGase F, EDTA free), ≥2.5 U/mL
- A recombinant form of PNGase F (100 mU, EDTA free), releases intact N-glycans by cleaving between the innermost GlcNAc and Asn.
- 5x N-glycanase reaction buffer,
- denaturation solution,
- detergent solution,
- 5x N-glycanase Tris reaction buffer (MS applications).
- Enzyme Specific Activity : ≥10 units/mg
- Volume : 40 µL
- Application : Glycoprotein deglycosylation
- pH Range : 7.5-9.5
- Enzyme Specificity
- Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless α(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.
- This product is Endo F free.
- 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 Unit Definition : One unit is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 μmole of denatured ribonuclease B per minute at 37°C, pH 7.5.
- Enzyme Formulation : 20 mM Tris-HCl, 50 mM NaCl, (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 asPNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
- Concentration : 2.5 U/mL
- Unit : 100 mU
- Molecular Weight : ~35,000 daltons
- pH Optimum : 8.6
*Available in different unit and packing size