α-Chymotrypsin from bovine pancreas
SIGMA/CHY5S - ≥40 units/mg protein, vial of 5 mg
Synonym: α-chymotrypsin A and B
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.
| biological source | bovine pancreas |
| composition | protein, ≥85% UV |
| description | aseptically filled |
| form | solid |
| mol wt | 25 kDa |
| packaging | vial of 5 mg |
| Quality Level | 200  |
| specific activity | ≥40 units/mg protein |
| storage temp. | −20°C |
| type | Type IV-S |
| UniProt accession no. | P00767  |
| Analysis Note: | Protein determined by A |
| Application: | α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers. |
| Application: | The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration. |
| Application: | α-Chymotrypsin from bovine pancreas has been used: • as a supplement for the collection of semen into Tris diluent • as one of the proteases in the analysis of major histocompatibility complex (MHC) class II protease sensitivity assay • as a component in YEPD broth for biofilm dispersion assay • in the preparation of chitinase–chymotrypsin–DM |
| 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. Its 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, 10 mM 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. |
| 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 |