Biochem/physiol Actions

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.

Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.

Caution

This product should be stored frozen at -20°C

Preparation Note

This is a 2.5 g/L porcine trypsin solution in Hank′s Balanced Salt Solution with phenol red.

Unit Definition

One BAEE unit will produce a A₂₅₃ of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.

Application

用于组织培养板上贴壁细胞的释放以进行传代。