Analytical Data
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Gene name
ATP5S
- Application
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Alternative Names
Atp5s; ATP5S_HUMAN; ATPW; FB; HSU79253
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99766
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Expression Region
1-127aa
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AA Sequence
MCCAVSEQRLTCADQMMLFGKISQQLCGVKKLPWSCDSRYFWGWLNAVFNKVDYDRIRDVGPDRAASEWLLRCGAMVRYHGQERWQKDYNHLPTGPLDKYKIQAIDATDSCIMSIGFDHMETSNICC
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Molecular Weight
39.71 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
ATP5S is a component of ATP synthase, an essential enzyme complex that plays a critical role in ATP production within the mitochondria of eukaryotic cells. The ATP synthase complex consists of multiple subunits, and ATP5S, specifically, is part of the stator region that stabilizes the structure and facilitates the conversion of ADP and inorganic phosphate into ATP through a proton gradient. Research on ATP5S and its role in cellular energy metabolism has gained significant interest due to its implications in understanding various metabolic disorders, mitochondrial dysfunction, and the aging process. Moreover, ATP synthase is a focal point in cancer research, given that altered energy metabolism is a hallmark of cancer cells. By studying the recombinant ATP5S protein, scientists aim to elucidate its structure, function, and interactions within the ATP synthase complex, providing insights into the mechanisms underlying its regulation in health and disease. The production of recombinant ATP5S allows for more detailed biochemical and biophysical studies, which can lead to the identification of potential therapeutic targets and strategies to modulate ATP synthesis in pathological conditions. This research not only enhances our understanding of mitochondrial biology but also holds promise for developing interventions in diseases linked to mitochondrial dysfunction.
