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C8946

Sigma-Aldrich

α-Chymotrypsin from human pancreas

lyophilized powder

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

lyophilized powder

Quality Level

mol wt

25 kDa

packaging

vial of ≥10 BTEE units

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CTRB1(1504)

General description

α-Chymotrypsin belongs to the trypsin family of serine proteases. It is secreted as an inactive precursor chymotrypsinogen to the intestine. The cleavage of peptide bond at amino acid 148 forms α-chymotrypsin. Chymotrypsinogen is encoded by the gene CTRB1 and is mapped to 16q23.1 in the human chromosome.

Application

α-Chymotrypsin from human pancreas has been used to test inhibition by N-alkyl isatins against mammalian serine proteases.
Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. Human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry.

Biochem/physiol Actions

A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the bond.

Unit Definition

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

Analysis Note

Protein determined by A1%/280

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

Genome-wide association study identifies inversion in the CTRB1-CTRB2 locus to modify risk for alcoholic and non-alcoholic chronic pancreatitis
Rosendahl J, et al.
Gut, 67(10), 1855-1863 (2018)
Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor
Mac Sweeney A, et al.
Acta Crystallographica Section D, Biological Crystallography, 56(3), 280-286 (2000)
Parallel synthesis of isatin-based serine protease inhibitors
Shuttleworth SJ, et al.
Bioorganic & Medicinal Chemistry Letters, 10(22), 2501-2504 (2000)
Sergey Y Vakhrushev et al.
Molecular & cellular proteomics : MCP, 12(4), 932-944 (2013-02-13)
Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor. Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered...
Liliane Schoofs et al.
Current pharmaceutical design, 8(7), 483-491 (2002-04-12)
The constant increase of life expectancy is associated with major ageing of developed populations. This indicates that the new century will have one of most epidemic progressions of cardiovascular, cancer and inflammatory diseases. The high challenge for medical research is...

Protocols

Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

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