C7752
Cytochrome c from equine heart
≥95% based on Mol. Wt. 12,384 basis
Synonym(s):
Cytochrome c from horse heart
Sign Into View Organizational & Contract Pricing
All Photos(5)
About This Item
Recommended Products
biological source
horse heart
Assay
≥95% (SDS-PAGE)
≥95% based on Mol. Wt. 12,384 basis
form
powder
mol wt
12,384
technique(s)
cell culture | mammalian: suitable
suitability
suitable for molecular biology
UniProt accession no.
storage temp.
−20°C
Gene Information
horse ... CYCS(100053958)
Looking for similar products? Visit Product Comparison Guide
Application
Cytochrome c is used as an inducer of mitochondria-dependent apoptosis in various research studies. The identification and monitoring of oxidation sites in cytochrome c may have implications for assessing oxidative stress-related conditions and diseases. It could potentially be used as a biomarker to evaluate the extent of oxidative damage and the antioxidant capacity of cells and tissues.
Cytochrome c is suitable for use as a component of phosphate buffer for the detection and evaluation of complex IV activity using blue-native gel electrophoresis (BN-PAGE). It may also be used for the detection of extracellular superoxide anion (ECSA) in isolated kidney phagocytes.
Cytochrome c is suitable for use as a component of phosphate buffer for the detection and evaluation of complex IV activity using blue-native gel electrophoresis (BN-PAGE). It may also be used for the detection of extracellular superoxide anion (ECSA) in isolated kidney phagocytes.
The specific sites and extent of oxidation in horse cytochrome c treated with H2O2 and UV were characterized. It was suggested that the state of these sites could be used as a biomarker for the oxidative environment in a cell.
Biochem/physiol Actions
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.
Cytochrome c is primarily known as an electron-carrying mitochondrial protein. The transition of cytochrome c between the ferrous and ferric states within the cell makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. It is generally regarded as a universal catalyst of respiration, forming an 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.
Application
Product No.
Description
Pricing
also commonly purchased with this product
Product No.
Description
Pricing
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Marilena Carbone et al.
Data in brief, 28, 104842-104842 (2019-12-24)
We present SEM, ThT fluorescence and circular dichroism (CD) data of amyloidogenic aggregates of cytochrome c (cyt c).This protein is of outmost relevance in many biochemical processes, such as respiratory chain in mitochondria and cells apoptosis. The present data focus
Dmitry Malyshka et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 23(5), 1151-1156 (2016-11-20)
Ferricytochrome c binding to cardiolipin-containing liposomes produces a heterogeneous distribution of conformations comprising native-like and non-native misfolded proteins. We utilized the photoreduction of native ferricytochrome c in the presence of potassium ferrocyanide and resonance Raman spectroscopy to probe the population of native
Lara Massai et al.
Journal of inorganic biochemistry, 165, 1-6 (2016-10-11)
Three Pd(II) and Pt(II) complexes with chelating mono(imidazolin-2-imine) and bis(imidazolin-2-imine) ligands i.e. [Pd(DMEAImiPr)Cl2] (1) (DMEAImiPr, 2-(1,3-diisopropyl-4,5-dimethylimidazolin-2-imine)ethan-1-dimethylamine), [Pd(DACH(ImiPr)2)Cl2] (2) (DACH(ImiPr)2, N,N'-(cyclohexane-1,2-diyl)bis(1,3-diisopropyl-4,5-dimethylimidazolin-2-imine)) and [Pt(DMEAImiPr)Cl2] (3), are evaluated here as potential cytotoxic and anticancer agents. An acceptable solution behaviour was found for the
A H Mulder et al.
Clinical and experimental immunology, 98(2), 270-278 (1994-11-01)
ANCA have been demonstrated to induce the respiratory burst in primed neutrophils. In this study we have extended the investigations on neutrophil activation by ANCA directed against proteinase 3 (PR3), myeloperoxidase (MPO) and lactoferrin (LF), and we have analysed the
Valentina Peleh et al.
BMC biology, 15(1), 106-106 (2017-11-10)
Many proteins of the mitochondrial intermembrane space (IMS) contain structural disulfide bonds formed by the mitochondrial disulfide relay. In fungi and animals, the sulfhydryl oxidase Erv1 'generates' disulfide bonds that are passed on to the oxidoreductase Mia40, which oxidizes substrate
Protocols
Enzymatic Assay of Superoxide Dismutase
Chromatograms
application for HPLCapplication for HPLCapplication for HPLCOur team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service