Analytical Data
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Gene name
ATP5H
- Application
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Alternative Names
ATP5H；ATP5H；ATP synthase subunit d. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75947
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Expression Region
1-161aa
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AA Sequence
AGRKLALKTIDWVAFAEIIPQNQKAIASSLKSWNETLTSRLAALPENPPAIDWAYYKANVAKAGLVDDFEKKFNALKVPVPEDKYTAQVDAEEKEDVKSCAEWVSLSKARIVEYEKEMEKMKNLIPFDQMTIEDLNEAFPETKLDKKKYPYWPHQPIENL
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Molecular Weight
45.4kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
ATP5H, also known as ATP synthase subunit h, is an essential component of the mitochondrial ATP synthase complex, which plays a crucial role in cellular energy production through ATP synthesis. In recent years, research has increasingly focused on the significance of ATP5H in various biological processes and disease states, including cancer, neurodegenerative disorders, and metabolic diseases. Its role in mitochondrial function and energy metabolism has raised interest in understanding how mutations or dysregulation of ATP5H can contribute to pathophysiological conditions. Recombinant ATP5H protein is invaluable for studying its structural and functional properties, allowing researchers to delve into its mechanistic functions in ATP synthesis and the broader implications for mitochondrial health. Such studies not only enhance our comprehension of mitochondrial biology but also pave the way for potential therapeutic interventions targeting mitochondrial dysfunctions associated with various diseases. Thus, the investigation of ATP5H through recombinant protein technology offers significant insights into its role in maintaining cellular energy homeostasis and its impact on human health.
