GKE-5010B
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Part Number:
GKE-5010B

Endoglycosidases

AdvanceBio N-Glycanase-plus (PNGase F), ≥10 U/mL (formerly ProZyme). Releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Includes 5x N-Glycanase reaction buffer:100 mM sodium phosphate pH 7.5, 0.1% sodium azide; denaturation solution: 2% SDS, 1 M 2-mercaptoethanol; detergent solution: 15% detergent; 5x N-Glycanase Tris reaction buffer: 50 mM Tris-HCl pH 8.0

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List Price:
$1,087.00

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Specifications
Enzyme Specific Activity
  • ≥10 units/mg
Volume
  • 40 µL
pH Range
  • 7.5-9.5
Enzyme Specificity
  • Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless a(1-3) core fucosylated, as in plant 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. Highly concentrated, is useful for deglycosylation under native conditions.
Enzyme Applications
  • To obtain efficient deglycosylation of glycoprotein substrates under nondenaturing conditions, it is necessary to use a higher starting concentration of enzyme. N-Glycanase-plus and ULTRA (EDTA-Free) are supplied at = 10 U/ml, and are recommended for all applications requiring deglycosylation of glycoproteins in the absence of denaturants. The high activity also allows smaller reaction volumes and shorter reaction times to be explored.
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 pH 7.5 and 37°C.
Enzyme Formulation
  • 20 mM Tris HCl pH 7.5, containing 1 mM EDTA and 50 mM NaCl
Enzyme Source
  • Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum. Enzyme also known as PNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
Concentration
  • 10 U/mL
Unit
  • 400 mU
pH Optimum
  • 8.6
Resources

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