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Merck

C4785

Sigma-Aldrich

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

Szinonimák:

Clostridiopeptidase A

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204

sterilitás

0.2 μm filtered

Forma

lyophilized powder

specifikus aktivitás

>1200 CDU/mg solid
2-5 FALGPA units/mg solid

molekulatömeg

68-130 kDa

alkalmasság

release of physiologically active rat pancreatic islets tested

tárolási hőmérséklet

−20°C

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Biokémiai/fiziológiai hatások

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.
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.

Egység definíció

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.

Elkészítési megjegyzés

Also contains clostripain, nonspecific neutral protease, and tryptic activities.
Prepared from Type XI (C7657)

szubsztrát

Product No.
Leírás
Árazás

Piktogramok

Health hazardExclamation mark

Figyelmeztetés

Danger

Figyelmeztető mondatok

Veszélyességi osztályok

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Az ügyfelek ezeket is megtekintették

Jörg Witthaut et al.
Clinical drug investigation, 31(11), 791-798 (2011-10-05)
Injectable collagenase Clostridium histolyticum is efficacious in correcting Dupuytren's contracture as assessed by changes in the angle of contracture and range of motion (ROM). However, clinically important changes in ROM have not been evaluated in depth. The objective of this
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
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
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

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