Recombinant Human Sorting Nexin 5

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-+/--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.

Pichia Pastoris.

The protein is formulated with 1mM HCl and 20mM CaCl2, pH-3.

IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQ VRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRA VINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAP VLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQ GVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS.

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).