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+1-617.299.7367 (Int’l)
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+1-888.733.6849
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| 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 | Escherichia Coli. |
| Physical Appearance | Sterile Filtered lyophilized powder. |
| Formulation | The protein was lyophilized with 10mM Sodium Acetate buffer and 50mM NaCl. |
| Solubility | It is recommended to reconstitute the lyophilized Human Trypsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. |
| Stability | Recombinant Human Trypsin althoµgh 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. |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Biological Activity | 10,000 BAEE units/mg powder. |
| Usage | NeoScientific'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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