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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

WGK 3

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
Chung Yeng Looi et al.
BMC complementary and alternative medicine, 13, 166-166 (2013-07-11)
Centratherum anthelminticum (L.) Kuntze (scientific synonyms: Vernonia anthelmintica; black cumin) is one of the ingredients of an Ayurvedic preparation, called "Kayakalp", commonly applied to treat skin disorders in India and Southeast Asia. Despite its well known anti-inflammatory property on skin
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
Esther Lapuente-Brun et al.
Science (New York, N.Y.), 340(6140), 1567-1570 (2013-07-03)
The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all
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