Cat: IPD-X41380

Recombinant SARS-CoV-2 E484K Protein (HEK293),His

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Analytical Data

  • Gene name

    E484K

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    E2 Peplomer protein

  • Species

    SARS-CoV-2

  • Source

    HEK293

  • Tag

    C- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0DTC2

  • Expression Region

    319-541aa(E484K)

  • Molecular Weight

    27.9 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 E484K mutation in the spike protein of the SARS-CoV-2 virus has garnered significant attention in the field of virology and vaccine research. Initially identified in various viral variants, including the Beta variant (B.1.351) and the Gamma variant (P.1), this mutation is located in the receptor-binding domain, which is critical for the virus's ability to attach to and enter human cells. The E484K mutation's emergence raised concerns about its potential to impact the effectiveness of neutralizing antibodies generated by previous infections or vaccinations. Studies have demonstrated that the E484K mutation can reduce the neutralization capacity of certain monoclonal antibodies and convalescent serum, thus posing a challenge to vaccination strategies. Researchers are actively investigating the structural and functional implications of this mutation, as well as its occurrence in vaccine breakthrough cases. Understanding the biological dynamics of the E484K variant is essential for developing updated vaccines and therapeutics, as well as informing public health responses to the evolving pandemic. The ongoing research into the E484K mutation exemplifies the broader efforts to monitor and respond to viral mutations that may affect transmission, virulence, and vaccine efficacy.

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