PNGase A cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.

• Cleaves N-glycans from plant and insect derived glycoproteins and glycopeptides
• Activity is not inhibited by an α1-3 Fucose residue on the chitobiose core
• Recombinant enzyme with no detectable exoglycosidase or other endoglycosidase contaminating activities
• Glycerol-free for optimal performance in HPLC and mass spectrometry analysis
• ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
• Optimal activity and stability for up to 24 months 

PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides. 

• Leaves N-glycan core oligosaccharides intact and suitable for further analysis
• Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
• ≥ 95% purity, as determined by SDS-PAGE and intact ESI-MS
• Stored in 50% glycerol
• Optimal activity and stability for up to 24 months
• Can be used under native or denaturing conditions

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Overview of Glycobiology