Recombinant Porcine Trypsin

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.

Recombinant Porcine Trypsin is expressed in E.coli and purified by standard chromatography techniques.

The Porcine Trypsin was lyophilized with mannitol as preservative.

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

Biological Activity: 4500 USP units/mg protein. One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25°C, with BAEE as a substrate (1cm light path) . Solubility: It is recommended to reconstitute the lyophilized Porcine Trypsin in sterile 1mM HCl or 50mM HAC not less than 100μg/ml, which can then be further diluted to other aqueous solutions.

VGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNI DVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA AAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGF LEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWI QQTIAAN.