C6423

α-Chymotrysin Protease

Cleaves at aromatic residues, suitable for mass spectrometry, from bovine pancreas

• CAS Number: 9004-07-3
• UNSPSC Code: 12352204
• eCl@ss: 42010112
• NACRES: NA.26
• EC Number: 232-671-2
• MDL number: MFCD00130481
• EC Number: 3.4.21.1 (BRENDA, IUBMB)

Properties

• Product Name: α-Chymotrypsin from bovine pancreas, suitable for protein sequencing, salt-free, lyophilized powder
• grade: Proteomics Grade
• Quality Segment: 200
• form: salt-free, lyophilized powder
• mol wt: 25 kDa
• technique(s): protein mass spectrometry: suitable
• suitability: suitable for protein sequencing
• UniProt accession no.: P00767
• storage temp.: 2-8°C
• Gene Information: cow ... CTRB1(618826)

Description

General description

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.

Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25.7 kDa and is widely used in pharmaceutical industry. It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.

Application

α-Chymotrypsin from bovine pancreas is used for the following applications:

• Protein Identification by mass spectrometry (MS)
• The isolation and characterization of myosin heavy chains
• Toxin preparation
• The incubation of infected and uninfected cells for analysis of cellular proteins by SDS-PAGE

α-Chymotrypsin from bovine pancreas (BPC) may be used as a catalyst in the preparation of tetrahydroquinoline derivatives by Povarov reaction.

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.

α-Chymotrypsin from bovine pancreas is stabilized by Ca²⁺ and catalyzes the hydrolysis of peptide bonds in particular the amino acids tyrosine, phenylalanine, tryptophan, and leucine at their C-terminal side. α-Chymotrypsin is inhibited by Cu²⁺ and Hg.

Other Notes

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

Safety Information

• Pictograms: GHS08,GHS07,GHS09
• Signal Word: Danger
• Hazard Codes: H302,H315,H319,H334,H335,H400
• Precautionary Statements: P261 - P264 - P273 - P301 + P312 - P302 + P352 - P305 + P351 + P338
• Hazard Classifications: Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
• Target Organs: Respiratory system
• Storage Class: 11 - Combustible Solids
• WGK: WGK 1
• PPE (personal protective equipment): dust mask type N95 (US), Eyeshields, Faceshields, Gloves