|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||11749 Da|
|Other Names||Cytochrome c, CYCS, CYC|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Cytochrome C was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Cytochrome C Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.|
|Cellular Location||Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane|
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Provided below are standard protocols that you may find useful for product applications.
Cytochrome c is located in the mitochondria of all aerobic cells and is involved in the electron transport system that functions in oxidative phosphorylation. It accepts electrons from cytochrome b and transfers them to cytochrome oxidase. In the process, the iron of the heme group, which is identical to that of hemoglobin and myoglobin, shifts from the ferrous to the ferric state (1). Recent progress in studies on apoptosis has revealed that cytochrome c is a pro-apoptotic factor. It is released from its places on the outer surface of the inner mitochondrial membrane at early steps of apoptosis and, combining with some cytosolic proteins, activates conversion of the latent apoptosis-promoting protease pro-caspase-9 to its active form. Cytochrome c release can be initiated by the pro-apoptotic protein Bax. This process is blocked by the anti-apoptotic proteins Bcl-2 and Bcl-xL (2). Also, differences in amino acid composition of cytochrome c have also been used as markers of biochemical evolution.
1. Wojtczak L, et al. Postepy Biochem 52(2):122-8, 2006.
2. Skulachev VP, et al. FEBS Lett 423(3):275-80, 1998.
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