Cat: PA2000-5005

Recombinant Human fimG Protein,His

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Analytical Data

  • Gene name

    fimG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    fimG;Protein FimG

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P08190

  • Expression Region

    24-167aa

  • AA Sequence

    ADVTITVNGKVVAKPCTVSTTNATVDLGDLYSFSLMSAGAASAWHDVALELTNCPVGTSRVTASFSGAADSTGYYKNQGTAQNIQLELQDDSGNTLNTGATKTVQVDDSSQSAHFPLQVRALTVNGGATQGTIQAVISITYTYS

  • Molecular Weight

    22.3 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 fimbrial protein fimG is a significant focus of research in microbiology, particularly concerning its role in the pathogenicity of uropathogenic Escherichia coli (UPEC), a leading cause of urinary tract infections (UTIs). Fimbriae, which are hair-like appendages on the bacterial surface, facilitate adhesion to the host's uroepithelial cells, promoting colonization and persistent infection. FimG plays a crucial role in the assembly and stability of these fimbrial structures, as it is involved in the regulation of fimbrial gene expression and the organization of the fimbrial fibers. Recent studies have utilized recombinant protein techniques to express and purify fimG, enabling detailed structural and functional analyses. Understanding the molecular mechanisms by which fimG contributes to UPEC virulence not only provides insights into bacterial pathogenesis but also presents potential avenues for developing novel therapeutic strategies. By targeting fimbrial adhesins, researchers aim to create more effective treatments for UTIs, reducing the reliance on antibiotics and addressing the growing problem of antibiotic resistance. The ongoing research into fimG and fimbrial interactions underscores the significance of this protein in the broader context of bacterial infection and host interaction, highlighting the need for innovative approaches to combat UPEC-related diseases.

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