Cat: IPD-X40124

Recombinant Escherichia coli cfaB Protein ,His & SUMO

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Analytical Data

  • Gene name

    cfaB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CFA/I antigen (CFA/I pilin) (Colonization factor antigen I subunit B) (cfaB)

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0CK93

  • Expression Region

    24-170aa

  • Molecular Weight

    31.1

  • 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 recombinant CFAB (Colonization Factor Antigen B) protein has gained significant attention in the field of microbiology and immunology due to its crucial role in the pathogenesis of enterotoxigenic Escherichia coli (ETEC), a leading cause of bacterial diarrhea worldwide. ETEC adheres to the intestinal mucosa primarily through fimbrial adhesins, with CFAB being one of the key factors involved in this adhesion process. Understanding the structure and function of CFAB can provide insights into the molecular mechanisms of bacterial colonization and host-pathogen interactions. Additionally, CFAB has potential applications in vaccine development, as eliciting an immune response against this protein could offer protection against ETEC infections. Researchers have focused on the expression and purification of recombinant CFAB to study its properties and interactions with host cells. By utilizing techniques such as molecular cloning and expression systems, scientists aim to produce large quantities of CFAB for further analysis. This research not only enhances our understanding of ETEC pathogenesis but also lays the groundwork for developing novel therapeutic and preventive strategies against diarrheal diseases caused by this pathogen. The development of effective vaccines targeting CFAB could significantly reduce the morbidity and mortality associated with ETEC infections, particularly in vulnerable populations such as children in developing countries. Thus, the investigation of CFAB recombinant protein is of paramount importance in addressing global health challenges related to enteric diseases.

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