Protease S. aureus V8 for sequencing (endoproteinase-Glu-C)

Protease S. aureus V8 (also known as endoproteinase-Glu-C) is a serine protease specifically used for selective cleavage of proteins for amino acid sequence determination or peptide mapping. It specifically cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues when used in phosphate buffer. When used in ammonium bicarbonate buffer or ammonium acetate buffer cleavage is restricted to the carboxyl side of glutamic acid residues only. The enzyme exhibits maximal activity from pH 4.0 to 7.8. With these unique features, this enzyme is widely used in proteomic and biopharmaceutical research to improve sequence coverage in mass spectrometry for peptide mapping. The inhibitors of V8 protease are diisopropylfluorophosphate (DFP), α2-macroglobulin and Nα-P-tosyl-L-lysine chloromethyl ketone (TLCK). Activity Definition:  > 500 U/mg. One Unit causes a change of 0.001 A280 nm per minute at 37°C, pH 7.8 using casein as the substrate. Applications: Used for selective cl