C4011
Cytochrome c from pigeon breast muscle
≥95% based on Mol. Wt. 12,173 basis
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About This Item
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biological source
pigeon muscle (breast)
Assay
≥95% based on Mol. Wt. 12,173 basis
form
powder
technique(s)
cell culture | mammalian: suitable
storage temp.
−20°C
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Application
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.
Preparation Note
Prepared with acetic acid without using TCA.
Other Notes
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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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
Why is the reduction of NO in cytochrome c dependent nitric oxide reductase (cNOR) not electrogenic?
Margareta R A Blomberg et al.
Biochimica et biophysica acta, 1827(7), 826-833 (2013-04-27)
The membrane-bound enzyme cNOR (cytochrome c dependent nitric oxide reductase) catalyzes the reduction of NO in a non-electrogenic process. This is in contrast to the reduction of O2 in cytochrome c oxidase (CcO), the other member of the heme-copper oxidase
Alexander N Volkov et al.
Biochemistry, 52(13), 2165-2175 (2013-03-23)
Here we present the preparation, biophysical characterization, and nuclear magnetic resonance (NMR) spectroscopy study of yeast cytochrome c peroxidase (CcP) constructs with enhanced solubility. Using a high-yield Escherichia coli expression system, we routinely produced uniformly labeled [(2)H,(13)C,(15)N]CcP samples with high
Chris L Bergstrom et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(16), 6269-6274 (2013-04-12)
The release of cytochrome c from mitochondria is a key signaling mechanism in apoptosis. Although extramitochondrial proteins are thought to initiate this release, the exact mechanisms remain unclear. Cytochrome c (cyt c) binds to and penetrates lipid structures containing the
Gongquan Li et al.
Biochemical and biophysical research communications, 434(4), 809-814 (2013-04-25)
Small-molecule Bcl-2/Bcl-xL inhibitor Navitoclax represents a promising cancer therapeutic since preclinical and clinical studies with Navitoclax have demonstrated strong anticancer activity in several types of cancers. However, because Navitoclax has a low binding affinity to Mcl-1, anticancer activity by Navitoclax
Chromatograms
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