Name: rPNGase F Glycosidase, 40000u, Mass Spectra Grade
Price: 324.00 USD

- Overview
  - PNGase F (Peptide:N-Glycosidase F) specifically hydrolyzes the amide bond between asparagine residues and N-linked oligosaccharides in complex or high-mannose-type glycoproteins. The reaction converts asparagine to aspartic acid through deamidation, releasing intact N-glycans while leaving the deglycosylated protein backbone undamaged. PNGase F does not remove oligosaccharides containing core α(1→3)-linked fucose. It is ideal for preparing glycoprotein and glycan samples for mass spectrometry analysis.
    
    Physical Form: 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA solution
    Shelf Life: Stable for 12 months at 4°C
    pH Range: Active over pH 6.0–10.0; optimal activity at pH 8.6
    Application: Specific cleavage of N-linked oligosaccharides from glycoproteins
    
    Enzymatic Digestion SOP:
    · Dissolve 20 µg of glycoprotein in 50 mM ammonium bicarbonate buffer (pH 7.8) and adjust total volume to 18 µL.
    · Add 2 µL of reconstituted PNGase F.
    · Incubate at 37°C for 2–18 hours.
    
    Cleavage Sites: R
    
    Please contact us at for specific academic pricing.
- Properties
  - Storage
    
    Store at 4–10°C in a refrigerator. Do not freeze below –20°C.
    
    Concentration
    
    10 unit/ul
    
    Molecular Weight
    
    36kDa.
    
    * For Research Use Only.
- Applications
  - Application Description
    
    Applied for protein identification, characterization of post-translational modifications, peptide mapping of biotherapeutic drugs, and de novo protein sequencing.

rPNGase F Glycosidase, 40000u, Mass Spectra Grade

rPNGase F Glycosidase, 40000u, Mass Spectra Grade

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