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Chymotrypsin from human pancreas
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GRADE & PURITY ≥95%(SDS-PAGE)
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Why this grade
≥95%(SDS-PAGE) for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
Storage & shipping
Store at -20°C Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
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.
Specifications
Product Name
Chymotrypsin from human pancreas
Specifications & Purity
≥95%(SDS-PAGE)
Biochemical and Physiological Mechanisms
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 h
Molecule Type
Enzyme
Storage and Shipping
Storage
Store at -20°C
Shipped In
Ice chest + Ice pads
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
Download SDS →✅ Certificate of Analysis (COA)
Lot-specific quality data. Enter your lot number to retrieve the exact COA.
Look up COA →🔬 Specification Sheet
Full quality attributes and acceptance criteria for this grade.
View spec sheet →Advanced Data
Certificates（CoA,COO,BSE/TSE and Analysis Chart)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Documents & Articles
Solution Calculators
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