Cat: IPD-X40325

Recombinant Escherichia coli uspD Protein ,His

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Analytical Data

  • Gene name

    uspD

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    yiiT

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0AAB8

  • Expression Region

    1-142aa

  • Molecular Weight

    20.4 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

The study of the uspD (universal stress protein D) recombinant protein has gained significance in the field of molecular biology and microbiology due to its potential role in bacterial stress response mechanisms. UspD is part of a family of universal stress proteins that are conserved across various bacterial species, suggesting a fundamental role in their survival and adaptability to adverse environmental conditions, such as nutrient depletion, oxidative stress, and extreme temperatures. Research has shown that UspD is upregulated under stress conditions, indicating its involvement in cellular protection and repair processes. Understanding the structure and function of UspD can provide insights into the molecular pathways that bacteria employ to cope with environmental challenges. Additionally, since bacterial stress responses are linked to pathogenicity and antibiotic resistance, unraveling the mechanisms of UspD may contribute to the development of novel therapeutic strategies. By characterizing uspD and producing its recombinant form, researchers aim to explore its biochemical properties and interactions with other cellular components, which could also enhance our knowledge of bacterial physiology and inform approaches to combat bacterial infections. This area of investigation not only addresses fundamental questions in microbiology but also holds practical implications for biotechnology and medicine.

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