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C2867

Sigma-Aldrich

Cytochrome c from equine heart

BioUltra, ≥99% (SDS-PAGE), powder, suitable for mammalian cell culture

Synonym(s):

CYC, CytC, Cytochrome c from horse heart

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

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

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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

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

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)

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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);
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
Han Xie et al.
Redox biology, 53, 102340-102340 (2022-05-25)
Generation of reactive oxygen species (ROS) are possibly induced by the crosstalk between mitochondria and endoplasmic reticula, which is physiologically important in apoptosis. Cytochrome c (Cyt c) is believed to play a crucial role in such signaling pathway by interrupting

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