Analytical Data
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Gene name
atpD
- Application
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Alternative Names
(ATP synthase F1 sector subunit beta)(F-ATPase subunit beta)
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Species
Lactobacillus reuteri
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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
A5VIR1
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Expression Region
1-475aa
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Molecular Weight
59.1 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
ATP synthase is a crucial enzyme complex that plays a vital role in cellular energy production through ATP generation in both prokaryotic and eukaryotic organisms. The atpD gene encodes the beta subunit of ATP synthase, which is essential for its catalytic function. Research on the recombinant expression of ATP synthase's components, including atpD, has garnered significant attention due to its potential applications in biotechnology and medicine. Understanding the structure and function of ATP synthase can provide insights into the mechanisms of energy regulation within cells, contributing to the development of novel bioenergetic therapies and bioengineering applications. Additionally, studies involving the recombinant production of the atpD protein can facilitate the exploration of the enzyme's activity, regulatory mechanisms, and interactions with other subunits. By generating and characterizing recombinant atpD protein, researchers aim to elucidate its role in ATP synthesis, the effects of mutations on enzyme performance, and potential strategies for therapeutic intervention in metabolic diseases linked to ATP production dysregulation. Overall, the exploration of atpD and its encoded protein holds promise for advancing our understanding of cellular bioenergetics and enhancing biotechnological applications, thereby underscoring its significance in both fundamental research and applied sciences.
