Analytical Data
-
Gene name
ATP5a
- Application
-
Alternative Names
ATP5A1; ATP5AL2; ATPM; OMR; ORM; hATP1
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P25705
-
Expression Region
Gln44~Ile526
-
Molecular Weight
56kDa
-
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
ATP5a is a vital component of the ATP synthase enzyme complex, which plays a crucial role in cellular energy production through oxidative phosphorylation in mitochondria. Research into ATP5a has gained importance due to its implications in various physiological and pathological processes, including metabolic disorders, neurodegenerative diseases, and cancer. Dysfunction in ATP5a can lead to impaired ATP synthesis, contributing to the energy deficit observed in these conditions. Additionally, ATP5a has been implicated in enhanced oxidative stress and inflammation, further complicating disease mechanisms. Given its central role in mitochondrial function, ATP5a is a promising target for therapeutic interventions aimed at improving mitochondrial health and function. Recent advances in recombinant protein technology have allowed for the production of ATP5a in sufficient quantities for structural and functional studies. By investigating the molecular mechanisms underlying ATP5a's role in ATP synthesis and its interactions with other mitochondrial components, researchers aim to uncover potential pathways for intervention and develop novel strategies for treating related diseases. This research not only enhances our understanding of cellular bioenergetics but also opens avenues for innovative therapeutic approaches in mitigating the effects of mitochondrial dysfunction.
