Chymotrypsin Sequencing Grade

Description

• General description: Chymotrypsin Sequencing Grade is isolated as a specific protease in pure form from bovine pancreas.
• Specificity: Serine endopeptidase that specifically hydrolyzes peptide bonds at the C-terminial of Tyr, Phe, and Trp. Leu, Met, Ala, Asp, and Glu are cleaved at a lower rate.[1] Acts also upon amides and esters of susceptible amino acids. The specificity of Chymotrypsin Sequencing Grade is tested with melittin as a substrate.
• Application: Use Chymotrypsin Sequencing Grade for the hydrolysis of proteins by chymotrypsin alone or in combination with other proteases.[2] It is suitable for peptide mapping, fingerprinting, and sequence analysis.
• Quality: Purity: Free of impurities that may interfere with the specific cleavage or separation of peptides in reversed-phase HPLC.
• Preparation Note: Working concentration: The recommended amount of enzyme is 1/200 to 1/20 of the quantity of protein by weight.Storage conditions (working solution): 2 to 8 °CA solution in 1 mM HCl can be stored for up to one week at 2 to 8 °C.Inhibitors: Aprotinin, DFP, PMSF, phenothiazine-N-carbonyl chloride, TPCK, ZPCK, α2-macroglobulin, α1-antitrypsin, soybean trypsin inhibitor, and chymostatin. No inhibition by APMSF.
• Reconstitution: Dissolve lyophilized chymotrypsin sequencing grade in 1mM HCl. The proteins to be sequenced are dissolved in digestion buffer (100mM Tris-HCl, 10mM CaCl2, pH 7.8).
• Other Notes: For life science research only. Not for use in diagnostic procedures.