C3483
Cytochrome c from human heart
≥95% (SDS-PAGE), lyophilized powder
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About This Item
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biological source
human heart
Quality Level
Assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
11 kDa by SDS-PAGE
technique(s)
cell culture | mammalian: suitable
mass spectrometry (MS): suitable
western blot (chemiluminescent): suitable
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... CYCS(54205) , CYCSL1(157317)
General description
Cytochrome c (CYCS) is mapped to human chromosome 7p15.3. CYCS is a heme protein containing three long α-helices. It undergoes domain swapping at the C-terminus and exists in dimeric, trimeric, and tetrameric forms. Insertion mutations in CYCS is implicated in acute myeloid leukemia. Mutations in CYCS modulates the release of proplatelets and decreases platelet production leading to thrombocytopenia 4.
Application
Cytochrome c from human heart has been used for the generation of standard curves in the electrochemiluminescence assay for measurement of cytochrome C levels in plasma samples and in electrospray ionization mass spectrum (ESI-MS) analysis.
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. Investigation on the effect of Paris Saponin I (PS I) on human gastric carcinoma cell growth (SGC7901 cells) have shown an elevated level cytoplasmic cytochrome c. Results are an inhibition of proliferation in SGC7901 cells by inducing mitochondria-dependent apoptosis through cytochrome c.
Biochem/physiol Actions
The ready fluctuation of cytochrome c within the cell between ferrous and ferric states, makes it an efficient biological electron-transporter. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal catalyst of respiration, it forms the essential electron-bridge between the respirable substrates and oxygen.
The ready fluctuation of cytochrome c within the cell between ferrous and ferric states, makes it an efficient biological electron-transporter. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal catalyst of respiration, it forms the essential electron-bridge between the respirable substrates and oxygen.
In addition to its function in electron transport, cytochrome c acts as an apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The two functions are finely tuned by phosphorylation of Tyr residues at position 48 and/or 97. One recent report provides suggestive evidence that phosphorylation at Tyr48 switches off the apoptotic effect.
In addition to its function in electron transport, cytochrome c acts as an apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The two functions are finely tuned by phosphorylation of Tyr residues at position 48 and/or 97. One recent report provides suggestive evidence that phosphorylation at Tyr48 switches off the apoptotic effect.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.
Preparation Note
Chemically oxidized during purification.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Ubiquinol (reduced Coenzyme Q10) in patients with severe sepsis or septic shock: a randomized, double-blind, placebo-controlled, pilot trial
Donnino MW, et al.
Critical Care, 19(1), 275-275 (2015)
5 `RUNX1-3?USP42 chimeric gene in acute myeloid leukemia can occur through an insertion mechanism rather than translocation and may be mediated by genomic segmental duplications
Zagaria A, et al.
Molecular Cytogenetics, 7(1), 66-66 (2014)
Cytochrome c polymerization by successive domain swapping at the C-terminal helix
Hirota S, et al.
Proceedings of the National Academy of Sciences of the USA, 107(29), 12854-12859 (2010)
Mutations of cytochrome c identified in patients with thrombocytopenia THC4 affect both apoptosis and cellular bioenergetics
De Rocco D, et al.
Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1842(2), 269-274 (2014)
Lin-Lin Gao et al.
World journal of gastroenterology, 17(39), 4389-4395 (2011-11-24)
To investigate the anti-tumor effects of Paris chinensis dioscin (PCD) and mechanisms regarding cell cycle regulation and apoptosis in human gastric cancer SGC-7901 cells. Cell viability was analyzed by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide assay. Cell apoptosis was evaluated by flow cytometry
Articles
Learn about the four membrane-bound protein complexes that make up the electron transport chain metabolic pathway supplying energy as ATP for cellular respiration.
Chromatograms
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