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Overview
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PNGase F is suitable for release of all types (high-mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGase F will not remove oligosaccharides containing α(1-3) linked core fucose commonly found on plant glycoproteins.
Recombinant PNGase F is isolated from a E. coli strain containing a clone of the Elizabethkingia miricola gene. There is no detectable difference in activity or specific activity of the recombinant enzyme from the native enzyme (E-PNG01).
PNGase F cleaves asparagine-linked (N-linked) oligosaccharides from glycoproteins. PNGase F deaminates asparagine to aspartic acid, leaving the oligosaccharides intact. Denaturation increases the rate of cleavage up to 100x. Most native proteins can still be completely N-deglycosylated but incubation time must be increased. PNGase F will remain active under incubation conditions for at least 72 hours. PNGase F will not remove oligosaccharides containing α(1,3)-linked core fucose commonly found on plant glycoproteins; for this purpose, use peptide N-glycosidase A.
Contents:
Ludger recombinant PNGase F - Kit contents
60 µL aliquot of recombinant PNGase F (0.3 U) in 20 mM Tris-HCl, pH 7.5
5x PNGase F Reaction Buffer 7.5 for PNGase F - 250 mM sodium phosphate, pH 7.5
PNGase F Denaturation Solution - 2% SDS, 1 M Beta-mercaptoethanol
PNGase F Triton X-100 - 15% solutionPlease contact us at for specific academic pricing.
More Details
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Overview