C2014
Collagenase from Clostridium histolyticum
0.2 μm filtered, Type V-S, ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid
Synonym(s):
Clostridiopeptidase A
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50 MG
₩169,810
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50 MG
₩169,810
About This Item
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Quality Level
sterility
0.2 μm filtered
form
lyophilized powder
specific activity
≥1 FALGPA units/mg solid
≥125 CDU/mg solid
mol wt
68-125 kDa
storage temp.
−20°C
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Application
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, lung epithelium and many other tissues. It is also effective in liver and kidney perfusion studies, digestion of pancreas, and isolation of nonparenchymal hepatocytes.
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.
Effective release of cells from tissue requires the action of both collagenase enzymes and the neutral protease. Collagenase is activated by four gram atom calcium (Ca2+) per mole enzyme. The culture filtrate is thought to contain at least 7 different proteases ranging in molecular weight from 68-130 kDa (pH optimum: 6.3-8.8). The enzyme recognizes the sequence -R-Pro-8-X-Gly-Pro-R-, where X is most often a neutral amino acid.
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
Prepared from Type V (C9263)
Analysis Note
Also contains clostripain, nonspecific neutral protease, and tryptic activities.
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary 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
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Mako Kato et al.
International journal of pharmaceutics, 423(2), 428-434 (2011-12-27)
Elevated interstitial fluid pressure (IFP) in a tumor is a barrier to tumor accumulation of systemic delivery of nanocarriers. In this study, we investigated whether intravenous injection of type I collagenase (collagenase-1) reduced IFP in tumors and increased the accumulation
Thomas J Edkins et al.
Journal of pharmaceutical and biomedical analysis, 70, 408-414 (2012-08-03)
This paper summarizes the development and validation of five enzyme activity methods to assess the specific inhibition of human endogenous matrix metalloproteinases MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin 1), MMP-8 (collagenase 2) and MMP-13 (collagenase 3) by anti-Collagenase
Beware of the small finger and/or the proximal interphalangeal joint? Skin lacerations following collagenase injection in dupuytren contracture.
Karsten Knobloch et al.
Plastic and reconstructive surgery, 130(1), 202e-204e (2012-06-30)
Ernest Azzopardi et al.
British journal of hospital medicine (London, England : 2005), 73(8), 432-436 (2012-08-10)
Dupuytren's disease is a common, costly and recurrent health issue. This review compares Clostridium histolyticum collagenase with current operative treatments. Collagenase management is an effective non-surgical alternative associated with lower risks of serious adverse events, but higher incidence of non-serious
A N Balamurugan et al.
Transplantation, 93(7), 693-702 (2012-02-10)
The optimal enzyme blend that maximizes human islet yield for transplantation remains to be determined. In this study, we evaluated eight different enzyme combinations (ECs) in an attempt to improve islet yield. The ECs consisted of purified, intact or truncated
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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