Cat: PA2000-2833

Recombinant Vibrio ctxB Protein,His

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Analytical Data

  • Gene name

    ctxB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ctxB;Cortexillin-2

  • Species

    Vibrio

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01556

  • Expression Region

    22-124aa

  • AA Sequence

    TPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN

  • Molecular Weight

    15.6 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

Recombinant ctxB protein, derived from the cholera toxin B subunit, has garnered significant attention in biomedical research due to its potential applications in vaccine development and immunotherapy. Cholera toxin, produced by the bacterium Vibrio cholerae, consists of an A subunit that is enzymatically active and a pentameric B subunit (ctxB) that binds to GM1 gangliosides on host cells, facilitating cellular entry of the A subunit. By studying ctxB, researchers aim to exploit its properties for enhancing mucosal immunity, an important aspect of vaccine design. Recombinant ctxB can be produced using various expression systems, such as bacteria or yeast, allowing for large-scale production and purification. This protein serves as an effective adjuvant when conjugated to antigens, enhancing their immunogenicity and promoting more robust immune responses. Furthermore, its role in drug delivery systems and cancer therapy has been investigated, as ctxB can target specific cells and facilitate the uptake of therapeutic agents. The ongoing research focuses on optimizing the efficacy and safety of ctxB-based vaccines and therapies, with the ultimate goal of improving public health outcomes in the face of infectious diseases.

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