PNGase F (500U/µL)

PNGase F (Peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidase) is a highly specific amidase that cleaves N-linked glycans from glycoproteins by hydrolyzing the bond between the asparagine residue and the innermost N-acetylglucosamine. It is active across a wide range of glycoproteins and efficiently releases high-mannose, hybrid, and complex N-glycans, except for structures containing α(1→3)-linked core fucose, commonly found in plant and insect glycoproteins.

This enzyme is provided at a high concentration of 500 U/µL, ensuring robust enzymatic activity even at low volumes. It functions efficiently in both native and denatured conditions, with optimal activity at pH 7.0–8.5 and temperatures between 25–37°C. In denaturing conditions, reducing agents such as DTT or β-mercaptoethanol are required to facilitate access to glycosylation sites. For native proteins, PNGase F activity can be influenced by steric hindrance and secondary structures, often necessitating mild denaturation for complete deglycosylation.

PNGase F is extensively used in glycoproteomic research, mass spectrometry-based glycan profiling, and structural analysis of glycoproteins. It is a critical tool in the biopharmaceutical industry for the characterization and quality control of recombinant glycoproteins, ensuring batch-to-batch consistency and verifying glycosylation patterns. The enzyme is recombinantly expressed to achieve high purity, stability, and lot-to-lot consistency.

Its ability to efficiently remove N-linked glycans makes PNGase F an essential reagent for researchers studying glycoprotein function, improving protein crystallization, and investigating post-translational modifications. It is widely used in workflows involving SDS-PAGE, Western blotting, and LC-MS/MS-based glycomic and proteomic analyses.