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C3131

Sigma-Aldrich

Cytochrome c from bovine heart

≥95% based on Mol. Wt. 12,327 basis, powder, suitable for mammalian cell culture

Synonym(s):

CYC, CytC

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About This Item

CAS Number:
9007-43-6
EC Number:
232-700-9
MDL number:
MFCD00130890
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine heart

Quality Level

200

Assay

≥95% based on Mol. Wt. 12,327 basis

form

powder

mol wt

12327 Da

storage condition

(Tightly closed Dry)

technique(s)

cell culture | mammalian: suitable

impurities

0.40-0.50% Iron (anhydrous)

solubility

water: 10 mg/mL, dark red-brown

UniProt accession no.

P00125

storage temp.

−20°C

Gene Information

cow ... CYC1(512500)

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General description

Research area: Apoptosis

Cytochrome c (Cyt C) is an essential mitochondrial protein located in the inner membrane of the mitochondria. It is encoded in the nucleus as apo-cytochrome C. Cyt C occurs as membrane-bound or as soluble metalloproteins in energy-transducing membranes and is found in bacteria, archaea, and plastids. It belongs to the group of class IIa cytochromes and contains pentacoordinate heme centres.

Application

Cytochrome C from bovine heart has been used:

  • as a component of the assay solution for testing the activity of respiratory chain complexes III and IV in the mitochondria of human osteosarcoma and human hepatocarcinoma cell lines
  • to determine the cytochrome c oxidase activity in mitochondria of human aortic endothelial cells
  • as a component of the cyt C oxidase reaction solution during in situ enzyme staining of cyt C oxidase in mice kidney tissues

Biochem/physiol Actions

Cytochrome C (Cyt C) is involved in the activation of caspase during the caspase-dependent apoptosis intrinsic pathway that triggers programmed cell death through apoptosis. It shows lipid-binding activity through its interaction with cardiolipin that accounts for the peroxidase activity of Cyt C. Cyt C binds to heme via the help of cytochrome c heme lyase that enables its release into the mitochondrial intermembrane space.
The ready interconversion of cytochrome c between ferrous and ferric states makes it an efficient biological electron carrier. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal link in the respiratory chain, 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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Increasing cGMP-dependent protein kinase I activity attenuates cisplatin-induced kidney injury through protection of mitochondria function
Hasiyeti M, et al.
American Journal of Physiology: Renal Physiology (2013)
Stéphane T Gabilly et al.
Frontiers in plant science, 8, 1313-1313 (2017-08-12)
Cytochromes c are hemoproteins, with the prosthetic group covalently linked to the apoprotein, which function as electron carriers. A class of cytochromes c is defined by a CXXCH heme-binding motif where the cysteines form thioether bonds with the vinyl groups
Yong-Ling P Ow et al.
Nature reviews. Molecular cell biology, 9(7), 532-542 (2008-06-24)
Cytochrome c is primarily known for its function in the mitochondria as a key participant in the life-supporting function of ATP synthesis. However, when a cell receives an apoptotic stimulus, cytochrome c is released into the cytosol and triggers programmed
C Garrido et al.
Cell death and differentiation, 13(9), 1423-1433 (2006-05-06)
In healthy cells, cytochrome c (Cyt c) is located in the mitochondrial intermembrane/intercristae spaces, where it functions as an electron shuttle in the respiratory chain and interacts with cardiolipin (CL). Several proapoptotic stimuli induce the permeabilization of the outer membrane
Chu-Chiao Wu et al.
Nature communications, 7, 13565-13565 (2016-11-25)
According to dogma, initiator caspases are activated through proximity-induced homodimerization, but some studies infer that during apoptosis caspase-9 may instead form a holoenzyme with the Apaf-1 apoptosome. Using several biochemical approaches, including a novel site-specific crosslinking technique, we provide the
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