Cytochrome C antibody

Cytochrome C is a small heme protein within the inner mitochondrial membrane responsible for carrying electrons within the respiratory transport chain.  Additionally, cytochrome c has also been identified as a player in programmed cell death (apoptosis). During the early phases of apoptotic death reactions, cytochrome c translocates from the mitochondria membrane into the cytoplasm and serves to trigger the apoptotic proteolytic cascade by activating caspase 3, through association with protease activating factor-1 (Apaf-1).

Cytochrome C is an electron carrier protein that localizes in mitochondrion intermembrane space and has been identified as one of the key signaling molecules of apoptosis or programmed cell death. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol.

Mitofilin was originally described as a heart muscle protein due to its high expression in the heart. Recently, analysis of the human heart mitochondrial proteome demonstrated that Mitofilin is one of the most abundant mitochondrial proteins (1). Researchers have reported finding two alternately spliced Mitofilin variants producing proteins of 88 and 90 kDa, that were detected in immunoblots with Mitofilin antibodies (2).

The caspases are a group of cysteine protease enzymes essential to apoptosis, inflammation and necrosis. Caspase 3 has been identified as one of the key mediators of apoptosis.