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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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.
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Twenty micrograms of various denatured glycoprotein standards were treated with 10 units of Promega recombinant or native PNGase F for 1 hour at 37°C. Gel shifts indicating deglycosylation were monitored by SDS-PAGE.
V4831 For Research Use Only. Not for Use in Diagnostic Procedures.