Sigma-Aldrich

CYTOCHROME C FROM BOVINE HEART (C005B-088513)

Name: CYTOCHROME C FROM BOVINE HEART (C005B-088513)
SKU: C005B-088513
Price: 349.98 USD
Availability: InStock

Cytochrome C is a heme protein. It is localized between the inner and outer mitochondrial membranes.

Description

General description

Cytochrome C is a heme protein. It is localized between the inner and outer mitochondrial membranes.

Application

Cytochrome c from bovine heart has been used:

for cytochrome oxidase staining using the mice brain tissue
as a component of control mixture to evaluate the accuracy of tandem mass spectra in identifying peptides
to study its effect on the stability, transport, and retention of biochar colloids (BCs) in saturated porous media under various solution pH and ionic strength (IS) conditions
as a component of staining solution for the detection of cytochrome oxidase activity in the brain tissue sections of mouse
as a component in the assay to study its superoxide scavenging efficiency
as a component of serum-free DMEM media to evaluate non-specific cytochrome C reduction in astrocytes and HT-29 cells

Biochem/physiol Actions

Cytochrome C is a key mediator of oxidative phosphorylation. It mediates the electron transport between complex III and complex IV of the respiratory chain.

Cytochrome c has been identified as an important mediator in apoptotic pathways. The release of mitochondrial cytochrome c into the cytoplasm stimulates apoptosis and is commonly used as an indicator of the apoptotic process in the cell. Investigation on the effect of Paris Saponin I (PS I) on human gastric carcinoma cell growth (SGC7901 cells) have shown an elevated level cytoplasmic cytochrome c. Results are an inhibition of proliferation in SGC7901 cells by inducing mitochondria-dependent apoptosis through cytochrome.

The ready interconversion of cytochrome c between ferrous and ferric states makes it an efficient biological electron carrier. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal link in the respiratory chain, it forms the essential electron-bridge between the respirable substrates and oxygen.