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C8946

Sigma-Aldrich

α-Chymotrypsin from human pancreas

lyophilized powder

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CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

human pancreas

Quality Level

form

lyophilized powder

mol wt

25 kDa

packaging

vial of ≥10 BTEE units

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CTRB1(1504)

Related Categories

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

Signal Word

Danger

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

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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Parallel synthesis of isatin-based serine protease inhibitors
Shuttleworth SJ, et al.
Bioorganic & Medicinal Chemistry Letters, 10(22), 2501-2504 (2000)
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)
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)
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
Sangram K Samal et al.
Acta biomaterialia, 9(9), 8192-8199 (2013-06-13)
The proteolytic enzyme α-chymotrypsin selectively cleaves the amorphous regions of silk fibroin protein (SFP) and allows the crystalline regions to self-assemble into silk microgels (SMGs) at physiological temperature. These microgels consist of lamellar crystals in the micrometer scale, in contrast

Protocols

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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