Analytical Data
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Gene name
ATP5J2
- Application
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Alternative Names
ATP5J2；ATP5J2；ATP5JL；ATP synthase subunit f. 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
P56134
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Expression Region
1-94aa
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AA Sequence
MASVGECPAPVPVKDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRGYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLKHERLRKYH
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Molecular Weight
12.4 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
ATP5J2, part of the ATP synthase complex, is a critical protein involved in ATP production within the mitochondria. Research on ATP5J2 has gained momentum due to its potential role in cellular energy metabolism and its implications in various diseases, including cancer and metabolic disorders. As a subunit of the F0 sector of ATP synthase, ATP5J2 facilitates the proton translocation necessary for ATP synthesis during oxidative phosphorylation. Its expression levels have been correlated with mitochondrial dysfunction, which is a hallmark of many pathologies. Consequently, understanding the functional dynamics of ATP5J2 through recombinant protein studies is crucial for elucidating its specific contributions to mitochondrial physiology and pathology. Furthermore, the production of recombinant ATP5J2 allows for in-depth biochemical characterization, exploration of protein-protein interactions within the ATP synthase complex, and the development of potential therapeutic strategies targeting mitochondrial dysfunction. These studies aim to provide insights into how manipulating ATP5J2 function could restore normal cellular energy levels and possibly reverse disease states associated with mitochondrial impairment. Overall, research on ATP5J2 not only advances our fundamental understanding of mitochondrial biology but also opens new avenues for therapeutic interventions aimed at improving cellular energy metabolism.
