PNGase F

PNGase F is a recombinant glycosidase cloned from Elizabethkingia miricola and overexpressed in E. coli. PNGase F has a molecular weight of 36kDa. 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 (Figure 1). PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins.

Unit Definition: One unit of PNGase F will catalyze the deglycosylation of 1 nanomole of denatured Ribonuclease B (RNase B) in one minute...

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PNGase F is a recombinant glycosidase cloned from Elizabethkingia miricola and overexpressed in E. coli. PNGase F has a molecular weight of 36kDa. 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 (Figure 1). PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins.

Unit Definition: One unit of PNGase F will catalyze the deglycosylation of 1 nanomole of denatured Ribonuclease B (RNase B) in one minute at 37°C. One Promega unit is equal to 1 IUB milliunit.

Molecular Weight: PNGase F has a molecular weight of approximately 36kDa.

Physical Form: PNGase F is supplied as a liquid in 20mM Tris-HCl (pH 7.5 at 25°C), 50mM NaCl and 5mM EDTA at a concentration of 10,000u/ml.

Applications

• Characterizing whether the protein is glycosylated (Figure 2).
• Determining the location of glycosylation on the protein (Figure 3).
• Characterizing the glycan structure.
• Protein trafficking.

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