GKE-5006A
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Endoglycosidases

Part Number:
GKE-5006A

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL (formerly ProZyme). A recombinant form of PNGase F, releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Includes 5x N-glycanase reaction buffer, denaturation solution, detergent solution, 5x N-glycanase Tris reaction buffer (MS applications). 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).

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List Price:
$314.00

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Specifications
Application
  • Glycoprotein deglycosylation
Concentration
  • ≥2.5 U/mL
Enzyme Applications
  • Preparation of deglycosylated proteins for molecular weight estimation or crystallography studies
  • Release of intact N-linked glycans from glycopeptides and glycoproteins
  • Structure-function studies of N-glycosylated glycoproteins
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 asPNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
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 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.
Molecular Weight
  • ~35,000 daltons
Unit
  • 100 mU
Volume
  • 40 µL
pH Optimum
  • 8.6
pH Range
  • 7.5-9.5
Literature
Data Sheets

Agilent AdvanceBio N-Glycanase

Agilent AdvanceBio N-Glycanase for the release of intact N-linked glycans for glycopeptides and glycoproteins and structure-function study of N-glycosylated glycoproteins.

  • Data Sheets
  • English
  • 30-Jul-2019
  • 588.50 Kb
  • PDF
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Support
Safety Data Sheets

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

  • Safety Data Sheets
  • English
  • 30-Apr-2019
  • 184.01 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

  • Safety Data Sheets
  • English
  • 30-Apr-2019
  • 160.92 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

  • Safety Data Sheets
  • English
  • 30-Apr-2019
  • 158.76 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/ml

  • Safety Data Sheets
  • English
  • 30-Apr-2019
  • 164.37 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), >2.5 U/mL

Material Safety Data Sheet

  • Safety Data Sheets
  • English
  • 25-Jan-2022
  • 552.18 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), >2.5 U/mL

Material Safety Data Sheet

  • Safety Data Sheets
  • English
  • 25-Jan-2022
  • 539.55 Kb
  • PDF

AdvanceBio N-Glycanase (PNGase F), >2.5 U/mL

Material Safety Data Sheet

  • Safety Data Sheets
  • English
  • 25-Jan-2022
  • 537.85 Kb
  • PDF

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