The PNGase F is a recombinant enzyme expressed in yeast, which can cleave high mannoses, heterozygotes, and complex oligosaccharide proteins linked by asparagine. The cleavage site of PNGase F is the amide bond between N-acetylglucosamine (GlcNAc) and asparagic acid residue on the inner side of the glycoprotein, and the aspartyl on the enzymatic hydrolysis protein is converted to aspartic acid. This product has a His tag and is often used for complete deglycosylation of antibodies and their related proteins. Component No. Name 20415ES01 20415ES02 20415-A PNGase F 15 KU 75 KU 20415-B1 Buffer 1(10×) 150 μL 750 μL 20415-B2 Buffer 2(10×) 300 μL 1500 μL 20415-B3 10% NP-40 300 μL 1500 μL Specifications Name PNGase F Source Expressed in Yeast Molecular weight 36 kDa Specific activity 750000 U/mL Buffer 20 mM Tris-HCl pH 7.5, 50 mM NaCl, 5 mM EDTA,50% Glycerol Unit Definition One unit is defined as the amount of enzyme required to remove > 95% of the carbohydrate from 10 µg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10 µL. Shipping and Storage The products are shipped with dry ice and can be stored at -15℃ ~ -25℃ for one year.