Cat: IPD-X41515

Recombinant Escherichia coli preT Protein ,His & Myc

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Analytical Data

  • Gene name

    preT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (DPD)(Dihydrothymine dehydrogenase)(Dihydrouracil dehydrogenase)

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P76440

  • Expression Region

    1-412aa

  • Molecular Weight

    51.8 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.

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Protein Description

PreT, a precursor protein, has garnered significant attention in the field of molecular biology due to its potential roles in various physiological processes and disease mechanisms. Research surrounding PreT focuses on its structure, function, and implications in pathologies such as neurodegenerative diseases and certain cancers. Notably, PreT is often implicated in the cellular stress responses and protein misfolding pathways, making it a critical subject of investigation. The protein's unique folding dynamics and interaction with other cellular components highlight its importance in maintaining cellular homeostasis. As scientists explore the mechanisms underlying PreT expression and activity, they aim to uncover its therapeutic potential and develop targeted interventions for diseases where PreT dysregulation plays a pivotal role. Understanding the molecular underpinnings of PreT could lead to novel biomarkers for early detection and innovative strategies for treatment, emphasizing the significance of continued research in this area.

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