α-Chymotrypsin from bovine pancreas
SIGMA/C4129 - Type II, lyophilized powder, ≥40 units/mg protein
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: C4129-10G
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: C4129-1G
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: C4129-250MG
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: C4129-500MG
| application(s) | diagnostic assay manufacturing |
| color | white to off-white |
| composition | protein, ≥85% |
| form | lyophilized powder |
| mol wt | 25 kDa |
| Quality Level | 300  |
| specific activity | ≥40 units/mg protein |
| storage temp. | −20°C |
| type | Type II |
| UniProt accession no. | P00767  |
| Analysis Note: | Protein determined by E |
| Application: | The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE). |
| 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, 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. |
| Other Notes: | View more information on chymotrypsin at www.sigma-aldrich.com/enz |
| Packaging: | 1, 10 g in poly bottle |
| Packaging: | 250, 500 mg in poly bottle |
| Preparation Note: | Produced from 3× crystallized chymotrypsinogen |
| 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 |