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cytochrome c oxidase subunit VIb polypeptide 2 (testis) ELISA Kits

Cytochrome c is a small, water-soluble protein of molecular weight about 12,000. It is a peripheral membrane protein of mitochondria. It is a heme protein that is localized in the compartment between the inner and outer mitochondrial membranes where it functions to transfer electrons between complex III and complex IV of the respiratory chain. It is electron carrier protein and its oxidized form 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. Cytochrome c is associated with specific binding sites on integral membrane proteins extending from the membrane surface.

Cytochrome c is approximately spherical in shape. The topology for the amino acids of this protein is typical of that normally found for water-soluble proteins. Polar amino acid residues largely reside on the outer surface of the protein, whereas hydrophobic amino acids are largely located in the interior of the protein. The hydrophobic effect is satisfied by this topology. As a result, cytochrome c is readily soluble in aqueous phase. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Cytochrome c is a key protein that initiates the intrinsic apoptosis pathway. Interestingly, cytochrome c itself undergoes antiapoptotic modification by glucose metabolism. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.

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