Trypsin Porcine

Others

Wet Ice

TRYPSIN

Lyophilized with mannitol as a preservative.
Physical Appearance: Sterile filtered white powder

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.

4, 500 USP units/mg protein.
Unit Definition: One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0 ml at pH 7.6 and 25° C, with BAEE as a substrate (1 cm light path).