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C2506

Cytochrome c from equine heart

≥95% (SDS-PAGE)

Synonym(s):

Cytochrome c from horse heart

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About This Item

CAS Number:
UNSPSC Code:
12352202
EC Number:
232-700-9
NACRES:
NA.61
MDL number:
Form:
powder
Assay:
≥95% (SDS-PAGE)
Biological source:
horse heart
Mol wt:
12,384
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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

horse ... CYCS(100053958)

Application

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.
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

Biochem/physiol Actions

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
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.

Preparation Note

Prepared using TCA.
This product in solution should be dark red to reddish brown when dissolved in water at 10 mg/mL.


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Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Articles

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

View All Articles

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)



Global Trade Item Number

SKUGTIN
C2506-1G04061835555864
C2506-50MG04061835555888
C2506-100MG04061835555857
C2506-250MG04061835543243
C2506-2G04061835521685
C2506-500MG04061835555871
C2506-5G04061835515868