Introduction and Features
Peptide N-Glycosidase F (PNGase F) is an amidase derived from Elizabethkingia miricola, genetically engineered for expression in Escherichia coli. This enzyme is the most effective enzymatic method for removing nearly all N-linked glycans from glycoproteins and plays a critical role in glycoprotein research. PNGase F cleaves N-linked glycans from glycoproteins, including high-mannose, hybrid, and complex-type oligosaccharides. The cleavage site is the glycosidic bond between the innermost N-acetylglucosamine (GlcNAc) of the glycan chain and the asparagine residue. In antibody glycosylation studies, obtaining accurate N-glycan profiles as quickly as possible is essential. Using the standard version of PNGase F, the release of N-glycans from antibodies typically requires several hours of incubation, followed by liquid chromatography or mass spectrometry analysis. PNGase F Fly is an improved reagent that enables rapid deglycosylation of antibodies within minutes. All N-glycans are released quickly and without bias, allowing for rapid glycoprofiling of glycosylated antibodies.
| Storage | At -18℃ or below for two years. |
| Shipping | Dry ice (-70℃) |
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