C2799
Colagenase
powder, suitable for cell culture, ≥4 FALGPA units/mg solid, high purity, ≥700 CDU/mg solid (CDU = collagen digestion units)
Sinônimo(s):
Clostridiopeptidase A
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About This Item
Produtos recomendados
fonte biológica
Clostridium histolyticum
Nível de qualidade
forma
powder
atividade específica
≥4 FALGPA units/mg solid
≥700 CDU/mg solid (CDU = collagen digestion units)
peso molecular
68-130 kDa
purificado por
chromatography
técnica(s)
cell culture | mammalian: suitable
pH
7.4
atividade externa
neutral protease and clostripain ≤1 unit/mg solid
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
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Aplicação
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.
Ações bioquímicas/fisiológicas
A colagenase é ativada por quatro gramas de átomos de cálcio por mol de enzima. Ela é inibida por ácido etileno glicol-bis(beta-aminoetil éter)-N, N, N′,N′-tetracético, beta-mercaptoetanol, glutationa, ácido tioglicólico e 8-hidroxiquinolina.
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.
Atenção
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.
Definição da unidade
Uma unidade de digestão de colágeno (CDU) libera peptídeos de colágeno do tendão de Aquiles bovino que equivalem em cor de ninidrina a 1,0 μmol de leucina em 5 horas em pH 7,4 a 37 °C na presença de íons de cálcio. Uma unidade de hidrólise de FALGPA hidrolisa 1,0 μmol de furilacriloil-Leu-Gli-Pro-Ala por min a 25 °C. Uma unidade de protease neutra hidrolisa caseína para produzir cor equivalente a 1,0 μmol de tirosina por 5 h em pH 7,5 a 37 °C. Uma unidade de clostripaína hidrolisa 1,0 μmol de BAEE por min em pH 7,6 a 25 °C na presença de DTT.
Nota de preparo
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.
produto relacionado
substrato
Nº do produto
Descrição
Preços
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órgãos-alvo
Respiratory system
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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Active site metal substitutions for both gamma- and zeta-collagenases from Clostridium histolyticum have been made by direct metal exchange. The incubation of Co(II), Cu(II), Ni(II), Cd(II), and Hg(II) with these native collagenases results in changes in activity that parallel those
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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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