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C2799

Sigma-Aldrich

Collagenase from Clostridium histolyticum

powder, suitable for cell culture, ≥4 FALGPA units/mg solid, high purity, ≥700 CDU/mg solid (CDU = collagen digestion units)

Synonym(s):

Clostridiopeptidase A

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.75

biological source

Clostridium histolyticum

Quality Level

form

powder

specific activity

≥4 FALGPA units/mg solid
≥700 CDU/mg solid (CDU = collagen digestion units)

mol wt

68-130 kDa

purified by

chromatography

technique(s)

cell culture | mammalian: suitable

pH

7.4

foreign activity

neutral protease and clostripain ≤1 unit/mg solid

shipped in

dry ice

storage temp.

−20°C

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Application

This product is suitable for the disaggregation of human tumor, mouse kidney, human adult and fetal brain, lung and many other epithelia tissues. It has also been shown to be effective in liver and kidney perfusion studies, digestion of pancreas, isolation of nonparenchymal rat liver cells and hepatocyte preparation. Collagenase has also been used in the preparation of arterial tissue for the study of Advanced Glycosylation End Products. This enzyme has been tested for the release of heptatocytes at a concentration of approximately 1 mg/mL. Concentrations for digestion range from 0.1 to 5 mg/mL.
Use for the digestion of collagen and the release of adherent cells from substrates.

Biochem/physiol Actions

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.
The collagenase product is a mixture of enzymes secreted by C. histolyticum, with different products differentiated by the relative ratios of the 10-18 components found in the secreted enzymes. The main components are two collagenases, clostripain, and a neutral protease. The synergistic action of these enzymes degrade collagen and other intracellular material. The action of both collagenase enzymes and the neutral protease is necessary for effective release of cells from tissue. Various types of collagen are the natural substrates for collagenase.

Caution

As supplied, this product is stable for one year at -20°C. There is no loss in FALGPA or protease activity in 30 days at 37°C, 50°C and -20°C. Solutions of crude collagenase are stable if frozen quickly in aliquots (at 10 mg/mL) and kept frozen at -20°C. Further freeze-thaw cycles will damage the solution. The product retains 100% activity over 7 hours when held on ice.

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.

Preparation Note

This collagenase is obtained from the culture filtrate of type VII (C0773) Clostridium histolyticum. The culture filtrate is thought to contain at least 7 different proteases ranging in molecular weight from 68-130 kDa. Solutions are typically prepared at 1-2 mg/mL in TESCA buffer (containing 50 mM TES, 0.36 mM Calcium chloride, pH 7.4 at 37°C.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

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

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Joseph E Peterson et al.
PloS one, 5(10), e13334-e13334 (2010-10-23)
Mineralized and permineralized bone is the most common form of fossilization in the vertebrate record. Preservation of gross soft tissues is extremely rare, but recent studies have suggested that primary soft tissues and biomolecules are more commonly preserved within preserved
Artificial intelligence-based comprehensive analysis of immune-stemness-tumor budding profile to predict survival of patients with pancreatic adenocarcinoma.
Zhou, et al.
Cancer Biology & Medicine, 20, 196-217 (2023)
Francisco Javier Rodríguez-Baena et al.
Scientific reports, 8(1), 13103-13103 (2018-09-01)
Recent advances have emphasized the relevance of studying the extracellular microenvironment given its main contribution to tissue homeostasis and disease. Within this complex scenario, we have studied the extracellular protease ADAMTS1 (a disintegrin and metalloprotease with thrombospondin motif 1), implicated
Tianxing Zhou et al.
Journal of experimental & clinical cancer research : CR, 42(1), 111-111 (2023-05-05)
Chemoresistance is the main reason for the poor prognosis of pancreatic ductal adenocarcinoma (PDAC). Thus, there is an urgent need to screen out new targets and compounds to reverse chemotherapeutic resistance. We established a bio-bank of human PDAC organoid models, covering a representative range of
E L Angleton et al.
Biochemistry, 27(19), 7406-7412 (1988-09-20)
Both gamma- and zeta-collagenases from Clostridium histolyticum are fully and reversibly inhibited by 1,10-phenanthroline at pH 7.5 in the presence of 10 mM CaCl2 with KI values of 0.11 and 0.040 mM, respectively. The inhibition is caused by removal of

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Discover pre-mixed collagenase enzyme blends with DNase I, Dispase II, Elastase, and Hyaluronidase and gently dissociate animal tissues in vitro.

Discover pre-mixed collagenase enzyme blends with DNase I, Dispase II, Elastase, and Hyaluronidase and gently dissociate animal tissues in vitro.

Discover pre-mixed collagenase enzyme blends with DNase I, Dispase II, Elastase, and Hyaluronidase and gently dissociate animal tissues in vitro.

Discover pre-mixed collagenase enzyme blends with DNase I, Dispase II, Elastase, and Hyaluronidase and gently dissociate animal tissues in vitro.

Protocols

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

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