α-Chymotrypsin from bovine pancreas
SIGMA/C7762 - Type I-S, essentially salt-free, lyophilized powder
Synonym: α-chymotrypsin A and B; alpha-chymotrypsin
CAS Number: 9004-07-3
EC Number: 232-671-2
MDL Number: MFCD00130481
Product Type: Chemical
α-Chymotrypsin is a serine protease of the peptidase S1 family consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues. α-Chymotrypsin is the predominant form of active enzyme produced from its zymogen, Chymotrypsinogen A.
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C7762-100MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: C7762-25MG
| form | essentially salt-free, lyophilized powder |
| mol wt | 25 kDa |
| purified by | 3× crystallization |
| Quality Level | 200  |
| solubility | 1 mM HCl: soluble 2.0 mg/mL, clear |
| specific activity | ≥40 units/mg protein |
| storage temp. | −20°C |
| type | Type I-S |
| UniProt accession no. | P00767  |
| Analysis Note: | Minimum 85% protein |
| Analysis Note: | Protein determined by E |
| Application: | α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin. |
| Application: | The product has been used to investigate the inhibitory effect of several ether oligomers against the enzyme. It has also been used to cleave pro-phenoloxidase in order to estimate total phenoloxidase in haemolymph. Furthermore, the enzyme has been used as a positive control in chymotrypsin assays using salivary gland and anterior midgut extracts of Deraeocoris nigritulus. |
| Biochem/physiol Actions: | α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, as well as 10 mM of Cu2+ and Hg2+. |
| Biochem/physiol Actions: | A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond. |
| Other Notes: | One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C. |
| Other Notes: | View more information on chymotrypsin at www.sigma-aldrich.com/enz |
| Packaging: | 5, 25, 100 mg in glass bottle |
| Preparation Note: | Prepared free of autolysis products and low molecular weight contaminants. |
| Preparation Note: | The powder may be reconstituted in 1 mM HCl at 2 mg/mL concentration to form a clear solution. |
| Symbol |    GHS07,GHS08,GHS09 |
| Signal word | Danger |
| Hazard statements | H302 - H315 - H319 - H334 - H335 - H400 |
| Precautionary statements | P261 - P273 - P301 + P312 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 |
| Hazard Codes | Xn |
| Risk Statements | 36/37/38-42 |
| Safety Statements | 22-24-26-36/37 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| activity | specific activity: ≥40 units/mg protein |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.21.1 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |