C2867
Cytochrome c from equine heart
BioUltra, ≥99% (SDS-PAGE), powder, suitable for mammalian cell culture
동의어(들):
CYC, CytC, Cytochrome c from horse heart
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Form:
powder
Assay:
≥99% (SDS-PAGE)
Biological source:
horse heart
Mol wt:
12,384
biological source
horse heart
Quality Level
product line
BioUltra
assay
≥99% (SDS-PAGE)
form
powder
mol wt
12,384
storage condition
(Tightly closed Dry)
technique(s)
cell culture | mammalian: suitable
solubility
water: 10 mg/mL, dark red-brown
UniProt accession no.
storage temp.
−20°C
Gene Information
horse ... CYCS(100053958)
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General description
Cytochrome C (Cyt C) is a nuclear DNA-encoded protein. It is derived from its precursor apo-cytochrome c and moves across the outer membrane of the mitochondria.
Research area: Apoptosis
Research area: Apoptosis
Application
Cytochrome c from equine heart has been used to prepare a stock solution for synthesizing and calibrating biotinylated cytochrome c. It has also been used as a component of the reaction buffer to stain electron transport chain (ETC) complex IV and determine its activity using blue-native gel electrophoresis.
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 (Cyt C) acts as a potent signaling molecule of apoptosis by activating caspase 3, a death protease. It plays a role in heme-binding with the help of cytochrome c heme lyase which facilitates its release into the mitochondrial intermembrane space. Cyt C also exhibits lipid-binding by interacting with cardiolipin, a phospholipid that initiates protein unfolding and activates the peroxidase function in Cyt C.
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
A further purification of C2506
Prepared using TCA.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Yuning Hong et al.
Journal of the American Chemical Society, 134(45), 18713-18723 (2012-10-17)
Interactions of cytochrome c (cyt c) with cardiolipin (CL) partially unfold the protein, activating its peroxidase function, a critical event in the execution of apoptosis. However, structural features of the altered protein species in the heterogeneous ensemble are difficult to
Bradford G Hill et al.
Free radical biology & medicine, 47(6), 675-683 (2009-06-17)
Protein thiol modifications occur under both physiological and pathological conditions and have been shown to contribute to changes in protein structure, function, and redox signaling. The majority of protein thiol modifications occur on cysteine residues that have a low pK(a);
Hao Zhang et al.
Journal of the American Heart Association, 11(11), e022853-e022853 (2022-06-04)
Background Myocardial iron deficiency (MID) in heart failure (HF) remains largely unexplored. We aim to establish defining criterion for MID, evaluate its pathophysiological role, and evaluate the applicability of monitoring it non-invasively in human explanted hearts. Methods and Results Biventricular
Luz P Blanco et al.
Arthritis & rheumatology (Hoboken, N.J.), 73(12), 2282-2292 (2021-05-14)
Neutrophil extracellular traps (NETs) are extracellular lattices composed of nucleic material bound to neutrophil granule proteins. NETs may play pathogenic roles in the development and severity of autoimmune diseases such as systemic lupus erythematosus (SLE), at least in part, through
Nadia Bertola et al.
Antioxidants (Basel, Switzerland), 12(5) (2023-05-27)
Fanconi anemia (FA) is a rare genetic disease characterized by a dysfunctional DNA repair and an oxidative stress accumulation due to defective mitochondrial energy metabolism, not counteracted by endogenous antioxidant defenses, which appear down-expressed compared to the control. Since the
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