Cat: IPD-X40209

Recombinant Salmonella typhimurium ompD Protein ,His & SUMO

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Analytical Data

  • Gene name

    ompD

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ompD; nmpC; STM1572; Outer membrane porin protein OmpD

  • Species

    Salmonella typhimurium

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P37592

  • Expression Region

    22-362aa

  • Molecular Weight

    53.6 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 study of recombinant OmpD (Outer Membrane Protein D) has gained significance due to its critical role in the outer membrane of Gram-negative bacteria, particularly in Escherichia coli. OmpD functions as a porin, facilitating the transport of small molecules across the bacterial cell membrane, thus playing a vital role in nutrient uptake and antibiotic resistance. Insights into its structure and function can enhance our understanding of bacterial physiology and pathogenicity. Research on recombinant OmpD focuses on characterizing its biophysical properties, understanding its interactions with potential inhibitors, and exploring its role in vaccine development. Additionally, as antibiotic resistance becomes an increasingly pressing global health issue, OmpD presents a target for novel antimicrobial strategies. The ability to produce OmpD in recombinant systems allows for extensive studies on its functionality, stability, and interactions at a molecular level, paving the way for innovative approaches to combat resistant bacterial strains and inform drug design. Overall, the exploration of recombinant OmpD represents a promising frontier in microbiology, with potential implications for therapeutic developments and enhanced understanding of bacterial behaviors.

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