Recombinant Human Trypsin-2

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.

Escherichia Coli.

The protein was lyophilized with 10mM Sodium Acetate buffer and 50mM NaCl.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Recombinant Human Trypsin although stable at room temp for 1 week, should be stored desiccated below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.