Trypsin Human Recombinant, Yeast Shipping:Ice Packs Introduction Trypsin (EC3.4.21.4) is part of the serine protease family. Trypsin cleaves lysine and arginine at the C-terminal side of the peptide. The hydrolysis rate is slower if an acidic residue is on either sides of the cleavage site and no cleavage occurs if a proline residue is on the carboxyl side of the cleavage site. Trypsin optimum pH is pH-7 to 9. Trypsin will also hydrolyze ester and amide linkages of synthetic derivatives of amino acids such as: benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl- L-arginine methyl ester (TAME), tosyl-L-arginine methyl ester, N-α-benzoyl-L-arginine p-nitroanilide (BAPNA), L-lysyl-p-nitroanilide, and benzoyl-L-tyrosine ethyl ester (BTEE). Serine protease inhibitors that inhibit recombinant trypsin include TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride), benzamidine, soybean trypsin inhibitor, and ovomucoid. Description Recombinant Human Trypsin is free from any animal and human sources. Recombinant Human Trypsin expressed in Yeast and purified by standard chromatography techniques. Recombinant Human Trypsin is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Human Trypsin is free from protease inhibitors such as PMSF and EDTA. Source Pichia Pastoris. Physical Appearance Sterile Filtered clear liquid solution. Formulation The protein is formulated with 1mM HCl and 20mM CaCl2, pH-3. Stability Recombinant Human Trypsin should be stored at 2-8?C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Biological Activity 2,500 BAEE units/mg powder. Amino Acid Sequence IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQ VRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRA VINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAP VLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQ GVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS. Usage >