PNGase F (Glycerol and EDTA Free), 500 U/μL
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Product Description
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, EDTAfree 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.
Properties and Storage
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Product: PNGase F (Glycerol and EDTA Free), recombinant (rDNA product)
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Source: E. coli strain expressing the PNGase F gene from Elizabethkingia miricola
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Molecular weight: ~36 kDa
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Enzyme type: N-Glycosidase F
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Function: Catalyzes cleavage of N-linked oligosaccharides between the innermost GlcNAc and asparagine residues of high-mannose, hybrid, and complex glycoproteins
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Specificity: Does not remove oligosaccharides containing α(1,3)-linked core fucose (commonly found in plant glycoproteins)
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Purity: ≥98% purity confirmed by 10% reducing SDS-PAGE
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Protein concentration: Determined by UV absorbance at 280 nm
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Unit definition: One unit removes >95% of carbohydrate from 10 µg of denatured glycoprotein
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Format: Glycerol-free and EDTA-free; suitable for HPLC, UPLC, and LC-MS glycoprotein analysis
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Enzyme: Store at 2–8 °C
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Buffers and reagents: Store at –20 °C
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Handling note: Spin tubes briefly before use
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Expiry: Refer to package for details
Application
- Characterization of glycoprotein
- Determining location of glycosylation on the protein
- Glycan structure determination
- Monoclonal antibody characterization