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C2139

Sigma-Aldrich

Collagenase from Clostridium histolyticum

suitable for release of rat epididymal adipocytes and hepatocytes (for methodology see Type II and Type IV), Type VIII, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid

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Synonym(s):
Clostridiopeptidase A
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

Clostridium histolyticum

Quality Level

type

Type VIII

form

powder

specific activity

≥125 CDU/mg solid
0.5-5.0 FALGPA units/mg solid

mol wt

68-125 kDa

suitability

suitable for release of rat epididymal adipocytes and hepatocytes (for methodology see Type II and Type IV)

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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General description

Clostridium histolyticum is a pathogenic clostridium that produces crude collagenases. This is a mixture of enzymes containing collagenase, non-specific proteases and clostripain.

Application

Collagenase may be used:
  • for the preparation of arterial tissue for the study of advanced glycosylation end products (AGE)
  • for use along with other proteases for the disaggregation of human tumor, mouse kidney, human brain, lung epithelium and many other tissues.
  • in liver and kidney perfusion studies, digestion of pancreas, and isolation of nonparenchymal hepatocytes.
  • for the preparation of viable hepatocytes from rat liver and for the isolation of fat cells from rat adipose tissue

Biochem/physiol Actions

Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(β-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, β-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline. Collagenase enzymes and neutral protease plays an important role in the effective release of cells from tissue. Collagenase recognizes the sequence -R-Pro-8-X-Gly-Pro-R-, where X represents a neutral amino acid.
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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Fleischer, S. and B. Fleischer
Methods in Enzymology, 192, 829-829 (1990)
Ce Tang et al.
Nature immunology, 19(7), 755-765 (2018-06-20)
The cytokines IL-17A and IL-17F have 50% amino-acid identity and bind the same receptor; however, their functional differences have remained obscure. Here we found that Il17f-/- mice resisted chemically induced colitis, but Il17a-/- mice did not, and that Il17f-/- CD45RBhiCD4+
Fleischer, S. and B. Fleischer
Methods in Enzymology, 173, 841-841 (1989)
Alan Moreira de Araujo et al.
Cells, 7(8) (2018-08-01)
Hepatocytes may rupture after a drug overdose, and their intracellular contents act as damage-associated molecular patterns (DAMPs) that lead to additional leukocyte infiltration, amplifying the original injury. Necrosis-derived DNA can be recognized as a DAMP, activating liver non-parenchymal cells (NPCs).
Parker, L.
Methods in Enzymology, 190, 480-480 (1990)

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.

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