Cat: PA2000-2341

Recombinant E.coli ystB Protein,His

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Analytical Data

  • Gene name

    ystB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ystB;Heat-stable enterotoxin B

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P74977

  • Expression Region

    53-71aa

  • AA Sequence

    EENDDWCCEVCCNPACAGC

  • Molecular Weight

    18.1 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

YstB is a protein of interest due to its role in various biological processes and potential applications in biotechnology and medicine. As a member of the Yersinia pestis multi-gene family, YstB is believed to play a significant role in the virulence of this pathogenic bacterium. Understanding the structure and function of YstB can provide insights into the mechanisms of disease caused by Yersinia species, thereby aiding in the development of therapeutic interventions. The recombinant expression of YstB allows researchers to study its properties in detail, enabling the investigation of its interactions with other cellular components and its impact on immune responses. Furthermore, YstB has been suggested as a candidate for vaccine development, promising to enhance protective immunity against infections caused by Yersinia. By harnessing advanced molecular biology techniques for the cloning and expression of the ystB gene, scientists can produce large quantities of the protein for detailed functional studies. This research not only advances our understanding of bacterial pathogenesis but also holds potential for the development of novel strategies to combat infectious diseases. The findings derived from YstB research could pave the way for innovations in vaccine design and therapeutic approaches, highlighting the protein's significance in both microbiological and medical research contexts.

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