In the experimental design, BTEE substrate was prepared, and 6 ul α-chymotrypsin of 0.2 mg/mL was added to the uartz cuvette with an optical path of 1cm of 2994 ul substrate and the absorption value of 256 nm was read every 10 seconds at 25 ℃.
Product Details
Product Details
Product Specification
Species | Human |
Synonyms | α-chymotrypsin A and B, alpha-chymotrypsin |
Expression System | E.coli |
Molecular Weight | 27 kDa (Reducing) |
Purity | >95% by SDS-PAGE and HPLC |
Tag | His Tag |
Physical Appearance | Lyophilized Powder |
Storage Buffer | 1 mM HCl, 2 mM CaCl2, pH 3.0 |
Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
Stability & Storage | Store at -25 ~ -15℃ for 2 years |
Reference | 1. Simon LM, Kotormán M, Garab G, Laczkó I. Structure and activity of alpha-chymotrypsin and trypsin in aqueous organic media. Biochem Biophys Res Commun. 2001 Feb 9;280(5):1367-71. PMID: 11162681. |
Background
Chymotrypsin is a serine endoproteinase that specifically cleaves peptide bonds at the C-termini of Tyr, Phe, Trp and Leu. Met, Ala, Asp and Glu may be cleaved at a much lower rate.
Components
Recombinant α-Chymotrypsin, human lyophilized powder
Protocol
Optimal incubation times and enzyme concentrations must be determined empirically for a particular substrate. Typical reaction conditions are as follows:
Add Recombinant α-Chymotrypsin, human, to a final protease: protein ratio of 1:200 to 1:20(w/w), and incubate sample for 2–18 hours at 25°C. The reaction may be stopped, if desired, by adding 0.5% trifluoroacetic acid.
Unit Definition
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Bioactivity

SDS-PAGE
1μg (R: reducing condition, N: non-reducing condition).
RP-HPLC
98.7%
