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.
序列
请咨询我们客服或者请查看品牌官方网站
来源宿主
大肠杆菌中重组表达
溶解建议
Sterile Filtered lyophilized powder. The protein was lyophilized without 10mM Sodium Acetate buffer and 50mM NaCl. It is recommended to reconstitute the lyophilized Human Trypsin in sterile 18MΩ-cm H2O not less than 100ug/ml， which can then be further diluted to other aqueous solutions.
保存建议
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.
