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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

Sinônimo(s):

CYC, CytC

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About This Item

Número CAS:
9007-43-6
Número CE:
232-700-9
Número MDL:
MFCD00130890
Código UNSPSC:
12352202
NACRES:
NA.61

fonte biológica

bovine heart

Nível de qualidade

200

Ensaio

≥95% based on Mol. Wt. 12,327 basis

Formulário

powder

peso molecular

12327 Da

condição de armazenamento

(Tightly closed Dry)

técnica(s)

cell culture | mammalian: suitable

Impurezas

0.40-0.50% Iron (anhydrous)

solubilidade

water: 10 mg/mL, dark red-brown

nº de adesão UniProt

P00125

temperatura de armazenamento

−20°C

Informações sobre genes

cow ... CYC1(512500)

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Descrição geral

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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 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 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.

Nota de preparo

Prepared with acetic acid without using TCA.

Outras notas

View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.

Aplicação

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Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

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Certificados de análise (COA)

Lot/Batch Number
SLBZ0555
SLBM4029V
SLBB6437V
031M7022
031M7022V

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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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Electron Transport

Learn about the four membrane-bound protein complexes that make up the electron transport chain metabolic pathway supplying energy as ATP for cellular respiration.

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

Chromatograms

application for HPLCapplication for HPLCapplication for HPLC

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