C4785
Collagenase from Clostridium histolyticum
0.2 μm filtered, release of physiologically active rat pancreatic islets tested, Type XI-S, 2-5 FALGPA units/mg solid, >1200 CDU/mg solid
Synonim(y):
Clostridiopeptidase A
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Numer CAS:
UNSPSC Code:
12352204
EC Number:
232-582-9
MDL number:
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Pomoc techniczna
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Pozwól nam pomócsterility
0.2 μm filtered
form
lyophilized powder
specific activity
>1200 CDU/mg solid, 2-5 FALGPA units/mg solid
mol wt
68-130 kDa
suitability
release of physiologically active rat pancreatic islets tested
storage temp.
−20°C
Quality Level
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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 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. The pH optimum is 6.3-8.8. The enzyme is typically used to digest the connective components in tissue samples to liberate individual cells. Collagenase treatment can cause some cells to die. Typically, concentrations varying from 0.1 to 5 mg/mL are used for digestion. The duration of reaction varies from 15 minutes to several hours and yields a satisfactory efficiency of cell dissociation without causing too much cell death. Krebs Ringer buffer with calcium and BSA is preferred and Zn2+ is required for activity. This enzyme is tested for suitability for the release of hepatocytes (at approx. 1 mg/mL in a total volume of 100 mL) for each rat liver.
Preparation Note
Also contains clostripain, nonspecific neutral protease, and tryptic activities.
Prepared from Type XI (C7657)
Other Notes
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.
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Numer produktu
Opis
Cennik
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Klasa składowania
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
M D Bond et al.
Biochemistry, 23(13), 3092-3099 (1984-06-19)
The relationship between the six collagenases (alpha, beta, gamma, delta, epsilon, and zeta) isolated and characterized in the preceding papers [Bond, M.D., & Van Wart, H.E. (1984) Biochemistry (preceding two papers in this issue)] has been investigated. Chemical modification reactions
A Endo et al.
Journal of biochemistry, 102(1), 163-170 (1987-07-01)
A collagenase active against native, insoluble collagen was isolated from the culture filtrate of a streptomycete which has been designated Streptomyces sp. C-51. Collagenase was produced by growing this strain in media containing gelatin. Purification by ammonium sulfate fractionation and
Thomas J Edkins et al.
Clinical and vaccine immunology : CVI, 19(4), 562-569 (2012-02-24)
Collagenase Clostridium histolyticum (CCH) contains a fixed ratio of class I (AUX-I) and class II (AUX-II) collagenases and is used as treatment for Dupuytren's contracture. These two Zn-dependent enzymes, produced by the Gram-positive bacterium Clostridium histolyticum, are related functionally to
Jörg Witthaut et al.
The Journal of hand surgery, 38(1), 2-11 (2012-12-12)
The JOINT I (United States) and JOINT II (Australia and Europe) studies evaluated the efficacy and safety of collagenase clostridium histolyticum (CCH) injection for the treatment of Dupuytren contracture. Both studies used identical open-label protocols. Patients with fixed-flexion contractures of
M C Heindl et al.
Biochimica et biophysica acta, 624(1), 51-59 (1980-07-24)
The recently isolated and purified collagenase produced by Achromobacter iophagus, the collagenase from Clostridium histolyticum, and thermolysin, three enzymes having common properties, were studied by circular dichroism. From the spectra of the aqueous solutions obtained in the peptide region, the
Active Filters
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