Analytical Data
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Gene name
ATP5J
- Application
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Alternative Names
ATP synthase; H+ transporting; mitochondrial F0 complex; subunit F6; ATP synthase-coupling factor 6; mitochondrial; ATP synthase-coupling factor 6; mitochondrial; ATP5; ATP5A; ATP5J; ATP5J_HUMAN; ATPase subunit F6; ATPM; CF6; F6
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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
P18859
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Expression Region
1-108aa
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Molecular Weight
36 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
Related Products
Protein Description
ATP5J, a subunit of ATP synthase, plays a crucial role in mitochondrial energy production by facilitating ATP generation from adenosine diphosphate (ADP) and inorganic phosphate. Research into ATP5J recombinant proteins has gained significant attention due to their potential therapeutic implications in metabolic disorders and mitochondrial dysfunction. Emerging evidence suggests that alterations in ATP5J expression can lead to impaired oxidative phosphorylation, contributing to various diseases, including neurodegenerative conditions and cancer. The development of recombinant ATP5J proteins enables detailed studies of its structure and function, providing insights into its role in ATP synthase assembly and stability. Additionally, these studies pave the way for exploring ATP5J as a potential target for drug development or gene therapy approaches aimed at restoring mitochondrial function. Investigating the biophysical properties and interactions of recombinant ATP5J can enhance our understanding of mitochondrial dynamics and energy metabolism, ultimately contributing to novel therapeutic strategies for preventing or treating diseases linked to mitochondrial dysfunction.
