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-a-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.
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毕赤酵母中重组表达
溶解建议
Sterile Filtered clear liquid solution. The Porcine Trypsin is formulated with 1mM HCl and 20mM CaCl2， pH-3.
保存建议
Recombinant Porcine Trypsin should be stored at 2-8C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）.
