The N-Glycosidase PNGase F is recombinant enzyme cloned from
Elizabethkingia miricola. It has molecular weight of ~36 Kda. PNGase F catalyzes the cleavage of N-linked oligosaccharides
between the innermost GlcNAc and asparagine residues of high mannose, hybrid and complex oligosaccharides from
N-linked glycoproteins. PNGase F will not remove oligosaccharides containing Alpha- (1,3)-linked core fucose commonly found
on plant glycoproteins. Glycerol free, EDTA free standard Buffer is preferred choice for HPLC, UPLC and LC-MS glycoprotein
samples.
Source: An E. coli strain that carries the gene which express PNGase F.

• Type: Recombinant N-Glycosidase from Elizabethkingia meningoseptica

• Molecular Weight: ~36 kDa

• Function: Cleaves N-linked oligosaccharides between GlcNAc and asparagine

• Specificity: Does not remove α(1,3)-linked core fucose (common in plant glycoproteins)

• Source: Expressed in E. coli

• Unit Definition: 1 unit removes >95% carbohydrate from 10 μg RNase B in 1 hour at 37°C

• Purity: >98% by 10% reducing SDS-PAGE

• Protein Concentration: Measured at UV 280 nm

• Storage: Store enzyme and all buffers at –20°C

• Handling: Spin tubes briefly before use; thaw buffers at room temperature before starting reactions

• Characterization of glycoprotein
• Determining location of glycosylation on the protein
• Glycan structure determination
• Monoclonal antibody characterization

• IdeS Protease, Lyophilized, Mass Spectrometry Grade, 50 U/μL
• Glu-C Sequencing Grade
• Antibody Standard for PNGase F
• Recombinant Carboxypeptidase B (Frozen, Glycerol-Free)
• EdnaQuickPNGase F Reaction Mix
• PNGase F (Glycerol and EDTA Free), 500 U/μL
• PNGase F, Glycerol-free, 500 U/μL
• Modified Trypsin, Lyophilized

Technical Data Sheet