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C8857

Sigma-Aldrich

ProteoMass™ Cytochrome c MALDI-MS Standard

vial of 10 nmol, (M+H+) 12,361.96 Da by calculation

Synonym(s):

Cytochrome c from equine heart, Cytochrome c from horse heart

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About This Item

CAS Number:
9007-43-6
MDL number:
MFCD00130890
UNSPSC Code:
12352202
NACRES:
NA.24

product line

ProteoMass™

Quality Level

100

form

solid

mol wt

(M+H+) 12,361.96 Da by calculation

packaging

vial of 10 nmol

technique(s)

mass spectrometry (MS): suitable

application(s)

cleaning products
cosmetics
flavors and fragrances
food and beverages
personal care

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Application

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.
Protein calibration standard for MALDI-MS instruments.

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

View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.

Legal Information

ProteoMass is a trademark of Sigma-Aldrich Co. LLC

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Storage Class Code

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WGK

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Flash Point(F)

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Flash Point(C)

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Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Chris L Bergstrom et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(16), 6269-6274 (2013-04-12)
The release of cytochrome c from mitochondria is a key signaling mechanism in apoptosis. Although extramitochondrial proteins are thought to initiate this release, the exact mechanisms remain unclear. Cytochrome c (cyt c) binds to and penetrates lipid structures containing the
Margareta R A Blomberg et al.
Biochimica et biophysica acta, 1827(7), 826-833 (2013-04-27)
The membrane-bound enzyme cNOR (cytochrome c dependent nitric oxide reductase) catalyzes the reduction of NO in a non-electrogenic process. This is in contrast to the reduction of O2 in cytochrome c oxidase (CcO), the other member of the heme-copper oxidase
Gabriel Ichim et al.
Molecular cell, 51(5), 632-646 (2013-09-17)
The neurotrophin receptor TrkC was recently identified as a dependence receptor, and, as such, it triggers apoptosis in the absence of its ligand, NT-3. The molecular mechanism for apoptotic engagement involves the double cleavage of the receptor's intracellular domain, leading
Lianet Monzote et al.
Experimental parasitology, 136, 20-26 (2013-11-05)
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Reiko Ban-Ishihara et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(29), 11863-11868 (2013-07-04)
Mammalian cells typically contain thousands of copies of mitochondrial DNA assembled into hundreds of nucleoids. Here we analyzed the dynamic features of nucleoids in terms of mitochondrial membrane dynamics involving balanced fusion and fission. In mitochondrial fission GTPase dynamin-related protein
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