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.
PNGase F activity is inhibited by SDS, therefore under denaturing conditions it is essential to have NP-40 present in the reaction mixture in a 1:1 ratio. PNGase F will not cleave N -linked glycans containing core ?1-3 Fucose (PNGase A must be used in this instance).
PNGase F activity is inhibited by SDS, therefore under denaturing conditions it is essential to have NP-40 present in the reaction mixture in a 1:1 ratio. PNGase F will not cleave N -linked glycans containing core ?1-3 Fucose (PNGase A must be used in this instance).
Contents PNGase F in 20 mM Tris-HCl, pH 7.5. Included with 20 µL and 60 µL pack sizes: 5x Reaction Buffer 7.5 – 250 mM sodium phosphate, pH 7.5 Denaturation Solution – 2% SDS, 1 M Beta-mercaptoethanol Triton X-100 – 15% solution. Specific Activity >25 U/mg. Activity 5 U/ml. Molecular weight 35,000 daltons. pH range 6-10, optimum 7.5. Protocol 1. Add up to 200 µg of.
PNGase F – Wikipedia, PNGase F – QA-Bio, PNGase F – Wikipedia, PNGase F – Wikipedia
