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C9263 Sigma-Aldrich

Collagenase from Clostridium histolyticum

release of physiologically active rat pancreatic islets tested, Type V, ≥1 FALGPA units/mg solid, >125 CDU/mg solid

Synonym: Clostridiopeptidase A



General description

Clostridium histolyticum collagenases (CCH) are classified into two types ; I and II. Both are a single polypeptide with molecular weight of 114kDa - 113kDa, respectively. CCH I contains tandem domains and CCH II contain single domain for collagen binding.


Collagenase from Clostridium histolyticum has been used in a study to investigate the degradation of collagen by the cariogenic bacteria, Streptococcus mutans. Collagenase from Clostridium histolyticum has also been used in a study to investigate the survivability of collagen micronetworks in the presence of collagenase.

Collagenase has been used in the preparation of arterial tissue for the study of Advanced Glycosylation End Products (AGE). The enzyme has also been used along with other proteases for the disaggregation of human tumor, mouse kidney, human brain, and lung epithelial tissues among several others. It is also effective in liver and kidney perfusion studies, digestion of pancreas, and isolation of nonparenchymal hepatocytes. The product has been used to digest forearm skin biopsies from Parkinson disease patients to grow human skin fibroblast primary cultures. The enzyme from Sigma has been used for rodent islet isolation in a study that assayed glucokinase functions.


100, 500 mg in glass bottle

Biochem/physiol Actions

Clostridium histolyticum collagenase (CCH) is a digestive enzyme acting particularly on collagen. It is useful in the treatment of Dupuytren′s contracture, fibroproliferative disorder.

Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(beta-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, beta-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline.

Unit Definition

One collagen digestion unit (CDU) liberates peptides from collagen from bovine achilles tendon equivalent in ninhydrin color to 1.0 μmole of leucine in 5 hours at pH 7.4 at 37 °C in the presence of calcium ions. One FALGPA hydrolysis unit hydrolyzes 1.0 μmole of furylacryloyl-Leu-Gly-Pro-Ala per min at 25°C. One Neutral Protease unit hydrolyzes casein to produce color equivalent to 1.0 μmole of tyrosine per 5 hr at pH 7.5 at 37°C. One Clostripain Unit hydrolyzes 1.0 μmole of BAEE per min at pH 7.6 at 25°C in the presence of DTT.

Analysis Note

Also contains clostripain, nonspecific neutral protease, and tryptic activities.

Safety & Documentation

Safety Information

GHS08  GHS08
Signal word 
Hazard statements 
Personal Protective Equipment 
NONH for all modes of transport
WGK Germany 
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable


Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles


Enzymes for Cell Detachment and Tissue Dissociation

Collagenase cleaves the peptide bonds in native, triple-helical collagen. Because of its unique ability to hydrolyze native collagen, it is widely used in isolation of cells from animal tissue. Colla...
BioFiles 2006, 1.2, 3.
Keywords: Anaerobic, Biochemistry, Cell biology, Cell culture, Diabetes, Digestions, Enzyme activity, Fermentation, Oxidations, Purification


Enzymatic Assay of Collagenase

The continuous spectrophotometric rate determination (A345, Light path = 1 cm) is based on the following reaction:
Keywords: Extinction coefficient

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Peer-Reviewed Papers


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C2014 Collagenase from Clostridium histolyticum, sterile-filtered, suitable for release of physiologically active rat pancreatic islets, Type V-S, ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid


Product #


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F5135 N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala

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