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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

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.

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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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
View All Related Papers

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HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX-NP5: Affect of pH

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX: Affect of Particle Size

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Protocols

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Chromatograms

application for HPLCapplication for HPLCapplication for HPLC

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