biological source
human
Assay
≥95% (SDS-PAGE)
form
lyophilized
mol wt
25 kDa
packaging
pkg of 100 μg
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... CTRC(11330)
General description
Chymotrypsin from human pancreas 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. It is secreted by the pancreas as inactive chymotrypsinogen C. Molecular weight of this enzyme is found to be 25kDa. The pI is 8.75.
Biochem/physiol Actions
Chymotrypsin from human pancreas selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan and leucine. Loss-of-function mutations in this gene have been associated with increased risk of chronic pancreatitis. It has high activity toward leucyl peptide bonds. The enzyme acts as a co-activator of procarboxypeptidases A1 and A2.
Physical form
Lyophilized as a salt-free solid.
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
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