The purification procedure of this product is based on literature references for chymotrypsin A. Therefore, it is believed to be Chymotrypsin A (or Alpha-Chymotrypsin). However, the product is not specifically tested for chymotrypsin B, C, or CTRL, so the presence of B, C, or CTRL cannot be ruled out.
C8946
α-Chymotrypsin from human pancreas
lyophilized powder
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About This Item
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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.[1] Chymotrypsinogen is encoded by the gene CTRB1 and is mapped to 16q23.1 in the human chromosome.[2]
Application
α-Chymotrypsin from human pancreas has been used to test inhibition by N-alkyl isatins against mammalian serine proteases.[3]
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
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
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 Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Mac Sweeney A, et al.
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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)
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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Does product number C8946, which is α-Chymotrypsin from the human pancreas, contain one or both of the three types of chymotrypsin produced by the human pancreas, namely chymotrypsin B form, chymotrypsin C, and the rarer form called "CTRL"?
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