Analytical Data
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Gene name
ATP5PB
- Application
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Alternative Names
ATP synthase peripheral stalk-membrane subunit b (ATP synthase proton-transporting mitochondrial F(0) complex subunit B1) （ATP synthase subunit b） （ATPase subunit b）
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P24539
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Expression Region
43-256aa
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Molecular Weight
32.1 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
ATP5PB, a subunit of the ATP synthase complex, plays a crucial role in the biosynthesis of adenosine triphosphate (ATP) in mitochondria. Research into ATP5PB is vital due to its implications in cellular energy production and its association with various diseases, including neurodegenerative disorders and cancer. Understanding the structure and function of ATP5PB helps elucidate the mechanisms by which ATP synthase operates, particularly in the context of mitochondrial dysfunction, which is a hallmark of many metabolic diseases. Recombinant ATP5PB protein studies facilitate the exploration of its biochemical properties, interactions with other mitochondrial components, and its regulatory mechanisms. Additionally, the recombinant form allows for the assessment of how mutations or alterations in ATP5PB can affect ATP synthesis and overall cellular health. This research not only contributes to the fundamental understanding of mitochondrial biology but also paves the way for potential therapeutic targets aimed at enhancing ATP production or mitigating the effects of mitochondrial diseases. Ultimately, the investigation of ATP5PB through recombinant protein techniques offers invaluable insights into energy metabolism and its broader implications for health and disease.
