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C7150

Sigma-Aldrich

Cytochrome c from equine heart

BioReagent, suitable for GFC marker

Synonym(s):

Cytochrome c from horse heart

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

product line

BioReagent

Quality Level

form

powder

mol wt

~12,400

packaging

vial of ≥10 mg

suitability

suitable for GFC marker

storage temp.

−20°C

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Application

Cytochrome c is primarily known as an electron-carrying mitochondrial protein and is generally regarded as a universal catalyst of respiration. Cytochrome c can be used as a gel filtration molecular weight marker in gel filtration chromatography and protein chromatography and can be used to study cytochrome c control proteins, electron transport and cellular respiration.
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 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

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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Federica Sinibaldi et al.
Journal of inorganic biochemistry, 105(11), 1365-1372 (2011-09-29)
In cells a portion of cytochrome c (cyt c) (15-20%) is tightly bound to cardiolipin (CL), one of the phospholipids constituting the mitochondrial membrane. The CL-bound protein, which has nonnative tertiary structure, altered heme pocket, and disrupted Fe(III)-M80 axial bond
Paolo Ascenzi et al.
Biochemical and biophysical research communications, 415(3), 463-467 (2011-11-08)
Carboxymethylation of equine heart cytochrome c (cytc) changes its tertiary structure by disrupting the heme-Fe-Met80 distal bond, such that carboxymethylated cytc (CM-cytc) displays myoglobin-like properties. Here, the effect of cardiolipin (CL) on peroxynitrite isomerization by ferric CM-cytc (CM-cytc-Fe(III)) is reported.
Kelly Watters et al.
PLoS pathogens, 14(12), e1007477-e1007477 (2018-12-12)
Viruses in the rhinovirus C species (RV-C) are more likely to cause severe wheezing illnesses and asthma exacerbations in children than related isolates of the RV-A or RV-B. The RV-C capsid is structurally distinct from other rhinoviruses and does not
Valentina La Verde et al.
Bio-protocol, 7(8), e2230-e2230 (2017-04-20)
Size exclusion chromatography (SEC) or gel filtration is a hydrodynamic technique that separates molecules in solution as a function of their size and shape. In the case of proteins, the hydrodynamic value that can be experimentally derived is the Stokes
Gongquan Li et al.
Biochemical and biophysical research communications, 434(4), 809-814 (2013-04-25)
Small-molecule Bcl-2/Bcl-xL inhibitor Navitoclax represents a promising cancer therapeutic since preclinical and clinical studies with Navitoclax have demonstrated strong anticancer activity in several types of cancers. However, because Navitoclax has a low binding affinity to Mcl-1, anticancer activity by Navitoclax

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