Description
Key facts
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Reacts with:Mouse, Rat, Cow, Human,
Form:LiquidSee storage information,
Storage buffer:Preservative: 0.02% Sodium azideConstituents: HEPES buffered saline
Product details:
The MitoBiogenesis™ western blotting cocktail (ab123545) is designed to study the regulation of mitochondrial biogenesis and cellular stress in response to environmental stimuli. It also can be used to monitor drug-induced effects on mitochondrial biogenesis. The two main components of this cocktail target two proteins, which are each subunits of a different oxidative phosphorylation enzyme complex, one subunit I of Complex IV (COX-I), which is mtDNA-encoded, and the 70kDa subunit of Complex II (SDH-A), which is nDNA-encoded. Complex IV includes several proteins which are encoded in the mitochondrion, while the proteins of Complex II are entirely encoded in the nucleus. An anti-Beta actin antibody is used as loading control.
Cocktail Antibodies:
Mouse CII-70 (SDHA) [2E3GC12FB2AE2] monoclonal
Amount: 25 μg
Working concentration: 0.5 μg/ml
Mouse CIV-1 (MT-CO1) [1D6E1A8] monoclonal
Amount: 50 μg
Working concentration: 1 μg/ml
Mouse Beta actin [mAbcam 8224] monoclonal
Amount: 25 μg
Working concentration: 0.5 μg/ml
**Antibody Purity:** Near homogeneity as judged by SDS-PAGE. The antibodies were produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation.**Related products**Review the , or the full to learn about more assays for metabolites, metabolic enzymes, mitochondrial function, and oxidative stress, and also how to assay metabolic function in live cells using your plate reader.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The combined target of SDHA COX1 and Beta-Actin involves three proteins with distinct mechanical roles in the cell. SDHA also known as succinate dehydrogenase subunit A exhibits a mass of approximately 70 kDa and functions as part of the mitochondrial complex II. COX1 or cytochrome c oxidase subunit 1 weighs around 57 kDa and is integral to the electron transport chain. Beta-Actin a cytoskeletal protein with a mass of about 42 kDa maintains cellular structure. SDHA and COX1 are expressed in mitochondria whereas Beta-Actin is found in the cytoplasm of most eukaryotic cells.
Biological function summary
SDHA helps convert succinate to fumarate in the Krebs cycle also known as the citric acid cycle as part of mitochondrial complex II. COX1 facilitates the transfer of electrons from cytochrome c to oxygen in mitochondrial complex IV. Beta-Actin plays roles in maintaining cell shape enabling cell motility and facilitating intracellular transport. Together SDHA and COX1 are involved in mitochondrial activities essential for energy production while Beta-Actin supports structural integrity.
Pathways
SDHA and COX1 significantly contribute to oxidative phosphorylation and the Krebs cycle important for energy metabolism. SDHA interacts with fumarate hydratase and succinate-coenzyme Q reductase in energy production pathways whereas COX1 works synergistically with other cytochrome c oxidase subunits. Beta-Actin is less involved in metabolic pathways and more associated with pathways governing cell movement and division interacting with proteins like myosin and tropomyosin.
SDHA and COX1 are implicated in mitochondrial dysfunctions such as Leigh syndrome and mitochondrial complex II deficiency. These disorders often lead to compromised energy metabolism and neurological symptoms. Beta-Actin abnormalities might relate to cancer metastasis due to its role in cell movement and structure. Disrupted interactions between these proteins and their pathways can result in altered cellular energy production and structural organization exacerbating disease conditions.
