Cat: IPD-X40137

Recombinant Borrelia burgdorferi fla Protein ,His & SUMO

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Analytical Data

  • Gene name

    fla

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    41 kDa antigen;P41

  • Species

    Borrelia burgdorferi

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P11089

  • Expression Region

    1-336aa

  • Molecular Weight

    51.8 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

Fla (flagellar) proteins are integral components of the bacterial flagellar apparatus, playing a crucial role in motility and pathogenesis. These proteins, particularly FlaA in many Gram-negative bacteria, are essential for the assembly and function of flagella, which are whip-like structures that enable bacteria to swim through liquid environments. Research into Fla proteins has gained considerable interest due to their implications in bacterial behavior and infection mechanisms. For instance, flagella are often associated with the virulence of pathogenic bacteria, facilitating adherence to host tissues and evasion of the immune response. Moreover, studies have shown that the structural and functional properties of Fla proteins can vary significantly across different species, highlighting their evolutionary significance. Understanding the molecular mechanisms underlying Fla protein assembly and regulation not only enhances our knowledge of bacterial mobility but also opens potential avenues for the development of novel therapeutic strategies aimed at disrupting bacterial motility and reducing infection rates. As antibiotic resistance continues to rise, targeting flagellar proteins presents a promising approach in the ongoing battle against bacterial infections. Thus, research on Fla proteins represents a vital intersection of microbiology, molecular biology, and medical science, driving efforts towards innovative solutions for public health challenges.

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