DescriptionApplications: Trypsin can be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form. Trypsin is commonly used in biological research.
Product Description: Trypsin consists of a single chain polypeptide of 223 amino acid residues. Trypsin is a member of the serine protease family.
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. 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.
Unit Definition: One unit hydrolyzes one µmole of TAME per minute at 25 °C, pH 8.2, in the presence of ionized calcium.
Typical Working Concentration: For the Removal of Adherent Cells from a Culture Surface: 2.5% w/v solution
|Proteins, Enzymes & Peptides|
|Dissolve blood clots|
|Optimum pH: Approximately 8.0(Lit.)|
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