Description

• Application: Highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-teminal 6x histidine fusion tag.
• Biochem/physiol Actions: Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
• Packaging: PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on doxorubicin cytotoxicity in human neuroblastoma cells.[1] It was used to treat a purified protein, mouse cone ultraviolet (MUV) pigment, before use in quantitative immunoblot analysis in a study[2] It is used to deglycosylate N-linked glycoproteins. Highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-teminal 6x histidine fusion tag.
• Unit Definition: One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit.