Analytical Data
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Gene name
ATP5H
- Application
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Alternative Names
ATP synthase D chain mitochondrial; ATP synthase H+ transporting mitochondrial F1F0 subunit; ATP synthase H+ transporting mitochondrial F1F0 subunit d; ATP synthase subunit d; ATP synthase subunit d; mitochondrial; ATP synthase; H+ transporting; mitochondrial F0 complex; subunit d; ATP5H; ATP5H_HUMAN; ATP5JD; ATPase subunit d; ATPQ; mitochondrial; My032 protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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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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Molecular Weight
45.4 kDa
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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
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Protein Description
ATP5H, a subunit of the ATP synthase complex, plays a crucial role in mitochondrial function by facilitating ATP production through oxidative phosphorylation. Research on ATP5H has gained interest due to its potential implications in various metabolic disorders and mitochondrial diseases, where impairments in ATP synthesis can lead to energy deficits and cellular dysfunction. Understanding the structure and function of ATP5H is essential for unraveling the mechanisms underlying these conditions. Recent studies have focused on the recombination and expression of ATP5H, utilizing techniques such as recombinant DNA technology and protein purification methods to produce this protein in sufficient quantities for functional assays. The characterization of recombinant ATP5H provides insights into its enzymatic activity, interaction with other subunits, and role in the overall ATP synthase assembly. Furthermore, exploring the relationship between ATP5H mutations and mitochondrial pathologies could pave the way for the development of targeted therapies aimed at restoring mitochondrial function or compensating for deficiencies. Overall, ATP5H research stands at the intersection of biochemistry and clinical relevance, offering promising avenues for therapeutic intervention in mitochondrial-related diseases.
