Genovis Inc. Immobilized PNGase F
Rapid and easy removal of N-glycans from antibodies and proteins using a spin column.
Immobilized PNGase F is a product in which the enzyme PNGase F (Peptide N-glycosidase F) is covalently bonded to agarose beads in a spin column format, allowing for the easy removal of N-glycans from antibodies, fusion proteins, and other N-glycosylated proteins. This enzyme is produced by expressing a gene derived from Elizabethkingia meningoseptica in E. coli through recombinant methods. Samples of glycoproteins are incubated with Immobilized PNGase F under standard reaction conditions for 1 hour to overnight, or under denaturing reaction conditions (using RapiGest SF Surfactant) for 15 to 60 minutes. The deglycosylated glycoproteins can then be easily collected by centrifugation. The activity of PNGase F on some glycoproteins may be reduced or inhibited due to steric hindrance. In such cases, longer incubation times or denaturation of the glycoproteins may be necessary.
basic information
●Characteristics of Immobilized PNGase F Enzyme PNGase F is a glycoamidase that hydrolyzes the amide bond between "asparagine of the polypeptide" and "the innermost GlcNAc of the oligosaccharide." It acts on complex, hybrid, and high-mannose type oligosaccharides that bind to asparagine in all mammals. Throughout the reaction, the asparagine residue from which the glycan has been removed is deaminated to aspartic acid. The released oligosaccharides remain intact and can be used for further analysis. The removal of N-glycans is widely utilized in sample preparation for MS analysis (reducing protein heterogeneity and enabling analysis of released glycans) and in the study of the functional roles of N-glycans. ●Genovis actively holds web meetings and seminars. Please feel free to contact us, and we will adjust according to your requests.
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Applications/Examples of results
Removal of N-glycans from antibodies, fusion proteins, and other N-glycosylated proteins.
