Cat: IPD-X41619

Recombinant Staphylococcus aureus esaB Protein ,His & Myc

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Analytical Data

  • Gene name

    esaB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Staphylococcus aureus

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0C050

  • Expression Region

    1-80aa

  • Molecular Weight

    16.6 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.

Quality inspection process

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Protein Description

The study of esaB recombinant protein has gained significant attention due to its role in bacterial pathogenesis and potential applications in biotechnology and medicine. EsaB, encoded by the esaAB operon, is predominantly associated with various bacterial species, particularly in the context of virulence and biofilm formation. Research indicates that esaB plays a pivotal role in regulating the expression of essential factors implicated in the infection process, thus influencing the host-pathogen interaction. Understanding the structure and function of esaB can provide insights into novel therapeutic targets for infectious diseases. Additionally, the recombinant production of esaB allows for the exploration of its biochemical properties and interactions in a controlled environment, facilitating the development of diagnostic tools and vaccines. Moreover, investigating the mechanisms of action of esaB could lead to advancements in genetically modified organisms for agricultural applications. As the demand for effective treatments against antibiotic-resistant bacterial strains increases, the characterization of esaB recombinant protein represents a promising avenue for innovative strategies in combating bacterial infections and enhancing food security. The ongoing research into this protein underscores the interplay between basic scientific inquiry and practical applications, highlighting the importance of esaB in both fundamental microbiology and applied sciences.

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