Cat: IPD-X40951

Recombinant Lemna minor atpB Protein ,His

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Analytical Data

  • Gene name

    atpB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ATP synthase F1 sector subunit beta

  • Species

    Lemna minor

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A9L9A3

  • Expression Region

    1-497aa

  • Molecular Weight

    57.5 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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

The ATPB gene encodes the β-subunit of ATP synthase, an essential enzyme that plays a crucial role in cellular energy production through oxidative phosphorylation and photophosphorylation. Research on recombinant ATPB protein has gained significant interest due to its central role in bioenergetics and potential applications in biotechnology. This protein is involved in the synthesis of adenosine triphosphate (ATP), the energy currency of cells, making it vital for various metabolic processes. Understanding the structure and function of recombinant ATPB can provide insights into the mechanisms of ATP synthesis and regulation. Additionally, studying its interactions with other subunits and regulatory proteins can enhance our knowledge of mitochondrial function and energy metabolism. Recombinant ATPB protein can also be utilized in various biotechnological applications, such as developing biosensors, studying enzyme kinetics, or engineering bioenergy-producing organisms. Advances in genetic engineering and protein purification techniques have facilitated the production of large quantities of ATPB, making it accessible for detailed biochemical studies. Furthermore, research into the polymorphisms and evolutionary aspects of the ATPB gene across different species can shed light on the evolutionary adaptations of energy metabolism in diverse environmental conditions. Overall, the study of recombinant ATPB protein holds promise for unraveling complex biochemical pathways, enhancing biotechnological innovations, and providing a deeper understanding of fundamental biological processes.

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