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About This Item
Form:
powder
Assay:
≥95% based on Mol. Wt. 12,327 basis
Biological source:
bovine heart
Mol wt:
12327 Da
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.
storage temp.
−20°C
Quality Level
Gene Information
cow ... CYC1(512500)
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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 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.
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.
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.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
Preparation Note
Prepared with acetic acid without using TCA.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Liang Cheng et al.
Biochemical and biophysical research communications, 477(4), 685-691 (2016-06-29)
Vascular lesions caused by endothelial dysfunction are the most common and serious complication of diabetes. The vasoactive potency of CTRP9 has been reported in our previous study via nitric oxide (NO) production. However, the effect of CTRP9 on vascular endothelial
Marina L Pridatchenko et al.
Analytical and bioanalytical chemistry, 402(8), 2521-2529 (2011-09-09)
The amino acid sequence determines the individual protein three-dimensional structure and its functioning in an organism. Therefore, "reading" a protein sequence and determining its changes due to mutations or post-translational modifications is one of the objectives of proteomic experiments. The
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
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
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