Analytical Data
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Gene name
MT-ATP6
- Application
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Alternative Names
(F-ATPase protein 6)
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Species
Chicken
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14092
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Expression Region
1-227aa
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Molecular Weight
26.3 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
MT-ATP6, a crucial component of the mitochondrial ATP synthase complex, plays a vital role in mitochondrial energy production. It encodes a subunit of ATP synthase located in the inner mitochondrial membrane, essential for ATP generation through oxidative phosphorylation. Research on MT-ATP6 has gained momentum due to its implications in various mitochondrial diseases and conditions, including neurodegenerative diseases, diabetes, and aging. Mutations in the MT-ATP6 gene have been linked to several pathogenic phenotypes, resulting in energy deficiency and contributing to the onset of mitochondrial disorders. The study of recombinant MT-ATP6 proteins enables researchers to explore the functional consequences of these mutations and their effects on ATP synthase activity. Additionally, understanding the structure and dynamics of MT-ATP6 is critical for developing therapeutic strategies aimed at restoring mitochondrial function in affected patients. Advances in recombinant protein expression and purification techniques have facilitated the detailed investigation of this protein, thereby providing insights into its role in bioenergetics and mitochondrial pathophysiology. This research not only enhances our comprehension of mitochondrial biology but also holds promise for developing innovative treatments for a spectrum of mitochondrial-related diseases. Overall, the continued exploration of MT-ATP6 and its recombinant forms is essential for elucidating the mechanisms of mitochondrial dysfunction and advancing potential therapeutic interventions.
