C6749
Cytochrome c equine
recombinant, expressed in E. coli
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About This Item
Productos recomendados
biological source
horse
Quality Level
recombinant
expressed in E. coli
assay
≥95% (SDS-PAGE)
form
powder
UniProt accession no.
storage temp.
−20°C
Gene Information
horse ... CYCS(100053958)
Application
Cytochrome c polymerization occurs by successive domain swapping, which may be a common mechanism of protein polymerization. Cytochrome c has been used in a study to establish that an optimized pulsed-Q dissociation and collision-activated dissociation hybrid workflow may have wide applications in biological and biomedical research.
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
Produced using animal component-free materials.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Ramil F Latypov et al.
Journal of molecular biology, 383(2), 437-453 (2008-09-02)
Despite close structural similarity, the ferric and ferrous forms of cytochrome c differ greatly in terms of their ligand binding properties, stability, folding, and dynamics. The reduced heme iron binds diatomic ligands such as CO only under destabilizing conditions that
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Coupling of multiplex isobaric tags for relative and absolute quantitation (iTRAQ) to a sensitive linear ion trap (LTQ) mass spectrometer (MS) is a challenging, but highly promising approach for quantitative high-throughput proteomic profiling. Integration of the advantages of pulsed-Q dissociation
Shun Hirota et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(29), 12854-12859 (2010-07-10)
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs at the early
Dorival Martins et al.
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Protocolos
Separation of HPLC protein standard mixture, analytical standard
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