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C2506

Sigma-Aldrich

Cytochrome c from equine heart

≥95% (SDS-PAGE)

Synonym(s):

Cytochrome c from horse heart

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About This Item

CAS Number:
9007-43-6
EC Number:
232-700-9
MDL number:
MFCD00130890
UNSPSC Code:
12352202

biological source

horse heart

Quality Level

300

Assay

≥95% (SDS-PAGE)

form

powder

mol wt

12,384

technique(s)

cell based assay: suitable

solubility

H2O: soluble 10 mg/mL

suitability

suitable for molecular biology

UniProt accession no.

P00004

application(s)

cell analysis

storage temp.

−20°C

Gene Information

horse ... CYCS(100053958)

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Application

Cytochrome c has been used:
  • in the reduction of ferricytochrome c by xanthine oxidase-generated superoxide radicals
  • as an analyte by the single droplet deposition method using MALDI mass spectra
  • as a terminal electron acceptor in the assay of standard cytochrome c reductase activity
  • in cytochrome c oxidase histochemistry
  • in the measurement of cytochrome C oxidase activity
  • as a component of phosphate buffer for the detection and evaluation of complex IV activity using blue-native gel electrophoresis (BN-PAGE)
  • for detection of extracellular superoxide anion (ECSA) in isolated kidney phagocytes
The specific sites and extent of oxidation in horse cytochrome c treated with H2O2 and UV were characterized. It was suggested that the state of these sites could be used as a biomarker for the oxidative environment in a cell.

Biochem/physiol Actions

Cytochrome c, released from the outer mitochondrial compartment into the cytosol aids in activation of caspase-9 and initiation of the apoptotic protease cascade. This process is facilitated through its interaction with apoptotic protease-activating factor-1 (APAF-1) and deoxyadenosine triphosphate (dATP).(3) Various studies suggest that measurement of cytochrome C level in serum of tumor patients can be considered as a potential marker for cell death in vivo.
Cytochrome c is primarily known as an electron-carrying mitochondrial protein. The transition of cytochrome c between the ferrous and ferric states within the cell makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. It is generally regarded as a universal catalyst of respiration, forming an essential electron-bridge between the respirable substrates and oxygen

Preparation Note

Prepared using TCA.

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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B C Hill
The Journal of biological chemistry, 266(4), 2219-2226 (1991-02-05)
The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen is measured by transient absorption spectroscopy. The oxygen reaction is initiated by photolytic removal of CO from cytochrome oxidase, using a flash-pumped dye laser. The subsequent reaction of the
Vittorio Pandini et al.
The Journal of biological chemistry, 277(50), 48463-48471 (2002-10-09)
Toxoplasma gondii possesses an apicoplast-localized, plant-type ferredoxin-NADP(+) reductase. We have cloned a [2Fe-2S] ferredoxin from the same parasite to investigate the interplay of the two redox proteins. A detailed characterization of the two purified recombinant proteins, particularly as to their
Enzyme-catalyzed free radical reactions with nicotinamide adenine nucleotides. II. Lactate dehydrogenase-catalyzed oxidation of reduced nicotinamide adenine dinucleotide by superoxide radicals generated by xanthine oxidase.
P C Chan et al.
The Journal of biological chemistry, 249(4), 1317-1319 (1974-02-25)
Attila I Gulyás et al.
The European journal of neuroscience, 23(10), 2581-2594 (2006-07-05)
Cytochrome c (CC) immunoreactivity was quantified in functionally distinct rat hippocampal inhibitory neuron populations using double immunocytochemistry and laser scanning confocal microscopy to measure the CC expression level as well as the amount of mitochondria within the cells, which is
Ian M Morison et al.
Nature genetics, 40(4), 387-389 (2008-03-18)
We report the first identified mutation in the gene encoding human cytochrome c (CYCS). Glycine 41, invariant throughout eukaryotes, is substituted by serine in a family with autosomal dominant thrombocytopenia caused by dysregulated platelet formation. The mutation yields a cytochrome
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