Analytical Data
-
Gene name
ATP5O
- Application
-
Alternative Names
Oligomycin sensitivity conferral protein ;OSCP
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P48047
-
Expression Region
24-213aa
-
Molecular Weight
47.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ATP5O, a gene encoding the ATP synthase subunit O, plays a crucial role in mitochondrial energy production through ATP synthesis. Located in the inner mitochondrial membrane, this subunit is vital for the proper assembly and function of the ATP synthase complex, which drives ATP generation during oxidative phosphorylation. Research on ATP5O has gained momentum due to its potential implications in various diseases associated with mitochondrial dysfunction, such as neurodegenerative disorders, cancer, and metabolic syndromes. Understanding the structure and function of ATP5O can provide insights into the mechanistic underpinnings of these diseases and facilitate the development of targeted therapies. Recombinant ATP5O protein studies enable researchers to analyze its biochemical properties, interactions with other mitochondrial proteins, and influence on ATP synthase activity. Moreover, investigating its role in cellular energy homeostasis and response to stress conditions can illuminate its importance in maintaining mitochondrial integrity. The study of ATP5O not only enhances our understanding of mitochondrial biology but also contributes to the broader field of bioenergetics and disease pathophysiology, emphasizing the need for further investigation into this essential protein.
