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Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.
Front Cell Neurosci. 2021 Oct 1;15:735723.
The Expression and Roles of the Super Elongation Complex in Mouse Cochlear Lgr5+ Progenitor Cells
Trypsin (porcine pancreas) purchased from AbMole
| Molecular Weight | 725.78 |
| Formula | C35H47N7O10 |
| CAS Number | 9002-07-7 |
| Solubility (25°C) | Soluble in water (10 mg/ml) Soluble in phosphate buffers (10 mg/ml) |
| Storage | 2-8°C, dry, sealed |
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