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). Apoptotic programmed death also involves the catalysis of lipid peroxidation in the mitochondria when cytochrome c is bound to acidic lipids such as cardiolipin.
Western Blot: Cytochrome C Antibody (7H8.2C12) [NB100-56503] - Analysis using cytochrome C antibody. Human HeLa lysate probed with cytochrome C antibody at 0.1 ug/ml.
Researchers from You's lab employed the cytochrome C antibody in their studies on lymphotoxin-beta receptor-mediated apoptosis by the Herpesvirus K7 and related survivin protein (1). To study the anti-apoptotic effects of the anti-inflammatory and anti-oxidant pigment curcumin, Chan's group used the cytochrome C antibody in photosensitized human epidermal carcinoma cells, and were able to demonstrate that the singlet oxygen ligand could trigger JNK, cytochrome c release, caspase activation, and apoptosis – a process which could be inhibited by curcumin (2). A follow-up study by the same group once again relied upon the cytochrome C antibody to demonstrate that a similar cell model challenged with the Rose Bengal (RB) photosensitizing agent responded in a similar fashion and was also curcumin-sensitive (3). Investigators at the South China Normal University used the cytochrome C antibody to establish the importance of the naturally occurring plant polyphenol resveratrol (RV) in Bak-dependent apoptosis in human lung adenocarcinoma cells (4). Furthermore, recent studies from Nogami's lab tested the death inducing properties on their novel, tailor-made designer helical peptides containing side-chain crosslinks based on the Bad protein binding domain (5). With the cytochrome C antibody, this group was able to demonstrate the formation of a stable complex between their synthesized helical peptides and Bcl-XL, as well as subsequent caspase activation and apoptosis.
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