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SRP6509 Sigma-Aldrich

Chymotrypsin from human pancreas

≥95% (SDS-PAGE)

Synonym: CLCR, CTRC, CTRC_HUMAN, Caldecrin, Chymotrypsin C, Chymotrypsin-C, ELA 4, Elastase 4, Elastase IV, Serum calcium decreasing factor

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Properties

biological source   human
assay   ≥95% (SDS-PAGE)
form   lyophilized
mol wt   25 kDa
packaging   pkg of 100 μg
UniProt accession no.   Q99895
shipped in   wet ice
storage temp.   −20°C
Gene Information   human ... CTRC(11330)

Description

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.

Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Target organs 
Respiratory system
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 1
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Protocols & Articles
Peer-Reviewed Papers
15

References

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