Recombinant Human Trypsin-2

Source : Escherichia Coli. Recombinant Human Trypsin-2 is free from any animal and human sources. Recombinant Human Trypsin-2 expressed in E.Coli having a Mw of 24kDa is purified by standard chromatography techniques. Recombinant Human Trypsin-2 is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Human Trypsin-2 is free from protease inhibitors such as PMSF and EDTA. 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- alpha-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.

It is recommended to reconstitute the lyophilized Human Trypsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. 10,000 BAEE units/mg powder.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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