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Product Description
Chymotrypsin 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. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine.
Biovision | 7538 | Chymotrypsin Human Pancreas DataSheet
Biomolecule/Target: Chymotrypsin
Synonyms: Caldecrin, Chymotrypsin C, Chymotrypsin-C, Chymotrypsin C, CLCR, CTRC, CTRC_HUMAN, ELA 4, ELA4, Elastase 4, Elastase IV, Elastase4, Elastase IV, Serum calcium decreasing factor
Alternates names: Caldecrin, Chymotrypsin C, Chymotrypsin-C, Chymotrypsin C, CLCR, CTRC, CTRC_HUMAN, ELA 4, ELA4, Elastase 4, Elastase IV, Elastase4, Elastase IV, Serum calcium decreasing factor
Taglines: A serine peptidase that selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine.
NCBI Gene ID #: 1270
NCBI Gene Symbol: CNTF
Gene Source: Human
Accession #: P26441
Recombinant: No
Source: Human Pancreas
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: N/A
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: 40-70 units per mg protein. One unit is defined as the amount of enzyme that hydrolyzes one µmole of Suc-Ala-Ala-Pro-Phe-pNA/min at 21°C, pH 8.0.
Results: 40-70 units per mg protein.
Binding Capacity: N/A
Unit Definition: One unit is defined as the amount of enzyme that hydrolyzes one µmole of Suc-Ala-Ala-Pro-Phe-pNA/min at 21°C, pH 8.0.
Molecular Weight: 25.0 kDa
Concentration: N/A
Appearance: Lyophilized
Physical form description: Lyophilized as a salt-free solid.
Reconstitution Instructions: N/A
Amino acid sequence: N/A
