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C2506

Sigma-Aldrich

Cytochrome c from equine heart

≥95% (SDS-PAGE)

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Synonym(s):
Cytochrome c from horse heart
CAS Number:
EC Number:
MDL number:

biological source

horse heart

Quality Level

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.

application(s)

cell analysis

storage temp.

−20°C

Gene Information

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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.

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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25G
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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

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  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. I see that you list several horse heart cytochrome c products. What are the differences, and which one should I choose?

    Product No. C2506 is prepared with trichloroacetic acid (TCA), whereas C7752 is prepared with the milder acetic acid. The TCA method may reduce the amount of superoxide dismutase (SOD) present, but tends to cause dimerization or acid-modified structures of cytochrome c. In contrast, acetic acid preparations may have slightly higher amounts of SOD, but a lower proportion of dimeric cytochrome c. So C2506 would be recommended for enzyme activity studies that require low SOD, whereas C7752 is recommended for structural studies or binding studies, or for enzyme activity studies where possible SOD contamination is not a problem. Product No. C2867 is prepared from C2506; it is a BioUtra grade product, greater than or equal to 99% pure as determined by SDS-PAGE. It is recommended when an ultra-high purity is required.  Product No. C3256 is also prepared from C7752; it is isolated by ion-exchange chromatography. This fraction shows a high rate of ascorbic acid oxidation, but low activity in a cytochrome oxidase system.  Product No. C7150 is also prepared from C7752; it is suitable for use as a gel filtration molecular weight marker.

  6. How do I determine how much of Product C2506, Cytochrome c, is in the oxidized form, and how much is reduced?

    This is determined by a spectral assay. The detailed assay procedure (operating procedure #11252) may be requested from Sigma St. Louis Technical Service (techserv@sial.com).

  7. Is Product C2506, Cytochrome c, predominantly in the oxidized form or the reduced form?

    This product is predominantly (>95%) in the oxidized form.

  8. How should I store solutions of Product C2506, Cytochrome c?

    Our general recommendations are as follows:  Store at -20 °C (freezer) for up to six months. Store at 2-8 °C (refrigerator) for up to two weeks. Store at 20-25 °C (room temperature) for up to three days. According to J. Biol. Chem, 237, 2161-2174 (1962), cytochrome c is stable to boiling, and over an unusually wide range of pH values. However, it denatures readily at extreme pH (low or high), and in high concentrations of organic solvents, such as ethanol or acetone.

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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Yamamoto FY, et al.
Fish & Shellfish Immunology, 77, 273-279 (2018)
A novel role of the mitochondrial permeability transition pore in (-)-gossypol-induced mitochondrial dysfunction
Warnsmann V, et al.
Mechanisms of Ageing and Development, 170, 45-58 (2018)
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)
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
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

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