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PNGase F
PNGase F cleaves the β-aspartylglucosamine bond between the N-Acetylglucosamine (GlcNAc) and asparagine linkage

PNGase F

Item Id: FSB0002
Your Price:
$119.00
Price and Availability
Amount
0.4 U [$119]
1.5 U [$419]
Quantity
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  • Description
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Recombinant PNGase F


Affinity purified, robust enzyme for N-linked glycan removal

Removal of N-linked glycans under denaturing or non-denaturing conditions. PNGase F, peptide N-glycosidase F, is a recombinantly expressed endoglycosidase from Flavobacterium meningosepticum that cleaves the β-aspartylglucosamine bond between the N-Acetylglucosamine (GlcNAc) and asparagine linkage of N-linked oligosaccharides in glycoproteins. This cleavage point acts as a convenient identification point in subsequent mass spectroscopy analysis.


Properties

Quantity0.4 U
Specific Activity>10 U/mg
Purity>95% by SDS-PAGE
Molecular Weight34,800 daltons (Apparent)
Extinction coefficient1 mg/ml = 2.01/cm path length (Calculated) at 280 nm
Theoretical pI8.39
StorageFormat: Liquid
Buffer: 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA
Temperature: 4C.
Stability: 1 year
Units One unit is defined as the amount of enzyme required to catalyze the release of >95% N-linked oligosaccharides from 60 μmoles of denatured ribonuclease B in 1 hour at 37C, pH 7.5. One micromolar unit of PNGase F activity is equal to 1,000 nanomolar units (IUB milliunits).


Supplied Reagents

  • Enzyme (stored in 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA)
  • 10X Deglycosylation Reaction Buffer (0.5 M sodium phosphate pH 7.5)





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