Cat: PA2000-2978

Recombinant E.coli yoaJ Protein,His

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Analytical Data

  • Gene name

    yoaJ

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    yoaJ;Expansin-YoaJ

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    C1P603

  • Expression Region

    1-24aa

  • AA Sequence

    MKKTTIIMMGVAIIVVLGTELGWW

  • Molecular Weight

    2.6 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 research on yoaJ, a gene found in various bacterial species, is gaining attention due to its potential role in protein interactions and cellular processes. YoaJ is believed to function as a regulator in stress response pathways, influencing how bacteria adapt to environmental changes. Preliminary studies suggest that the yoaJ protein may be involved in the biosynthesis of important metabolites and could modulate virulence factors in pathogenic strains. Understanding the structure and function of yoaJ recombinant proteins can provide insights into their mechanisms of action, potentially revealing targets for antibiotic development or novel therapeutic strategies. This research aligns with the broader goal of exploring microbial genetics and biochemistry to address emerging health threats and enhance biotechnological applications. The study of yoaJ could also contribute to our understanding of fundamental biological processes, making it a significant focus for researchers in the field of microbiology and molecular biology.

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