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C7752

Sigma-Aldrich

Cytochrome c from equine heart

≥95% based on Mol. Wt. 12,384 basis

Synonym(s):

Cytochrome c from horse heart

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

horse heart

Quality Level

assay

≥95% (SDS-PAGE)
≥95% based on Mol. Wt. 12,384 basis

form

powder

mol wt

12,384

technique(s)

cell culture | mammalian: suitable

suitability

suitable for molecular biology

UniProt accession no.

storage temp.

−20°C

Gene Information

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Application

Cytochrome c is used as an inducer of mitochondria-dependent apoptosis in various research studies. The identification and monitoring of oxidation sites in cytochrome c may have implications for assessing oxidative stress-related conditions and diseases. It could potentially be used as a biomarker to evaluate the extent of oxidative damage and the antioxidant capacity of cells and tissues.

Cytochrome c is suitable for use as a component of phosphate buffer for the detection and evaluation of complex IV activity using blue-native gel electrophoresis (BN-PAGE). It may also be used for the 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 has been identified as an important mediator in apoptotic pathways. The release of mitochondrial cytochrome c into the cytoplasm stimulates apoptosis and is commonly used as an indicator of the apoptotic process in the cell.
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 with acetic acid without using TCA.

Other Notes

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Ferricytochrome c binding to cardiolipin-containing liposomes produces a heterogeneous distribution of conformations comprising native-like and non-native misfolded proteins. We utilized the photoreduction of native ferricytochrome c in the presence of potassium ferrocyanide and resonance Raman spectroscopy to probe the population of native
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We present SEM, ThT fluorescence and circular dichroism (CD) data of amyloidogenic aggregates of cytochrome c (cyt c).This protein is of outmost relevance in many biochemical processes, such as respiratory chain in mitochondria and cells apoptosis. The present data focus
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Many proteins of the mitochondrial intermembrane space (IMS) contain structural disulfide bonds formed by the mitochondrial disulfide relay. In fungi and animals, the sulfhydryl oxidase Erv1 'generates' disulfide bonds that are passed on to the oxidoreductase Mia40, which oxidizes substrate
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ANCA have been demonstrated to induce the respiratory burst in primed neutrophils. In this study we have extended the investigations on neutrophil activation by ANCA directed against proteinase 3 (PR3), myeloperoxidase (MPO) and lactoferrin (LF), and we have analysed the

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Learn about the four membrane-bound protein complexes that make up the electron transport chain metabolic pathway supplying energy as ATP for cellular respiration.

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Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLCapplication for HPLCapplication for HPLC

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