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α-Chymotrypsin from bovine pancreas

SIGMA/C3142 - (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

Synonym: TLCK-Chymotrypsin

CAS Number: 9004-07-3
EC Number: 232-671-2
MDL Number: MFCD00130481
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-C3142-10MG 10 mg
$75.50
1/EA
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45-C3142-25MG 25 mg
$127.00
1/EA
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45-C3142-100MG 100 mg
$379.00
1/EA
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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: C3142-100MG

 

form essentially salt-free, lyophilized powder
mol wt 25 kDa
Quality Level 200 
solubility 1 mM HCl: soluble 10 mg/mL, clear
specific activity ≥40 units/mg protein
storage temp. −20°C
type Type VII
UniProt accession no. P00767 
Analysis Note: Protein determined by A1%/280
Application: α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.
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, 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/enzymeexplorer 
Packaging: 10, 25, 100 mg in glass bottle
Preparation Note: TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.
activity specific activity: ≥40 units/mg protein
Storage Temp. −20°C
Enzyme Commission (EC) Number 3.4.21.1   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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