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Our customer service representatives are available 24 hours, Monday through Friday to assist you.| Introduction | 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. |
| Synonyms | NULL |
| Source | Pichia Pastoris. |
| Physical Appearance | Sterile Filtered clear liquid solution. |
| Formulation | The protein is formulated with 1mM HCl and 20mM CaCl2, pH-3. |
| Stability | Recombinant Human Trypsin should be stored at 2-8C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). |
| Amino Acid Sequence | IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS. |
| Biological Activity | 2,500 BAEE units/mg powder. |
| Usage | NeoBiolab's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
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