Analytical Data
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Gene name
MT-ATP6
- Application
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Alternative Names
MT-ATP6；ATP6；ATPASE6；MTATP6；ATP synthase subunit a
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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
P00846
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Expression Region
1-226
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AA Sequence
MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSKIKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLAMSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT
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Molecular Weight
24.8kDa
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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 critical subunit of ATP synthase, plays a pivotal role in mitochondrial ATP production, which is essential for cellular energy metabolism. Research on MT-ATP6 has gained significant attention due to its association with various mitochondrial diseases and metabolic disorders, often resulting from mutations in the MT-ATP6 gene. These mutations can lead to impaired ATP synthesis, contributing to the pathogenesis of conditions such as Leigh syndrome, mitochondrial encephalomyopathy, and other neurodegenerative diseases. The study of MT-ATP6 recombinant proteins not only facilitates the understanding of its structure-function relationships but also aids in elucidating the mechanisms by which mutations disrupt normal mitochondrial function. Furthermore, recombinant MT-ATP6 proteins can serve as valuable tools for drug development and gene therapy approaches aimed at mitigating the effects of these mutations. Advances in techniques such as X-ray crystallography and cryo-electron microscopy have enabled researchers to visualize ATP synthase and its components in unprecedented detail, fostering insights into the conformational dynamics of the enzyme during ATP synthesis. Thus, understanding MT-ATP6 at the molecular level holds the potential to unlock new therapeutic avenues for mitochondrial diseases and improve strategies for mitochondrial gene therapy.
