Recombinant Human-α Chymotrypsin，Lyophilized

Description

α-Chymotrypsin is a serine protease capable of hydrolyzing the peptide bonds at the carboxyl - terminal ends of tyrosine, tryptophan, and phenylalanine. Ca²⁺ acts as both an activator and a stabilizer for α-chymotrypsin. This enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymotrypsin inhibitor, aprotinin, α₁-antitrypsin, α₂-macroglobulin, as well as 10 mM Cu²⁺ and Hg²⁺. Our recombinant human α-chymotrypsin is expressed in Pichia pastoris. It is obtained through multiple-step purification processes, ensuring freedom from contamination by other proteases.

• Unit definition: One unit (U) is defined as the amount of enzyme that hydrolyzes 1.0 μmol of BTEE per minute under the conditions of pH 7.8 and 25 °C.
• Reconstitution Solution：1mM HCl

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