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Cytochrome C Antibody

Rabbit Monoclonal Antibody

  • WB - Cytochrome C Antibody AJ1216b
    A. Western blot analysis on HeLa cell lysate using anti-Cytochrome C RabMAb (Cat. #AJ1216b).
  • IHC - Cytochrome C Antibody AJ1216b
    B. Immunohistochemical analysis of paraffin-embedded human heart muscle using anti-Cytochrome C RabMAb (Cat. #AJ1216b)
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P99999
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Monoclonal
Clone Names EP1326Y
Calculated MW 11749 Da
Gene ID 54205
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.
Dilution WB~~1:1000~10000
Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
StorageMaintain 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.
PrecautionsCytochrome C Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Synonyms CYC
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
Research Areas
Citations (0)

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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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Cat# AJ1216b
(40 western blots)
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