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C4011

Sigma-Aldrich

Cytochrome c from pigeon breast muscle

≥95% based on Mol. Wt. 12,173 basis

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CAS Number:
EC Number:
MDL number:
NACRES:
NA.61

biological source

pigeon muscle (breast)

Quality Level

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

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

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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
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
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
Xinliu Gao et al.
Archives of biochemistry and biophysics, 535(2), 197-204 (2013-04-17)
The filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus possesses an unusual electron transfer complex called Alternative Complex III instead of the cytochrome bc or bf type complex found in nearly all other known groups of phototrophs. Earlier work has confirmed that

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