Cat: IPD-X41168

Recombinant Influenza A virus M1 Protein ,His

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Analytical Data

  • Gene name

    M1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    /

  • Species

    Influenza A virus

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A0A2I8BGF8

  • Expression Region

    133-252aa

  • Molecular Weight

    19.3 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.

Quality inspection process

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Protein Description

The study of M1 recombinant proteins is rooted in the need to understand the intricate mechanisms of immune responses and viral pathogenesis. M1, a major protein component of certain viruses, plays a critical role in viral assembly and budding, influencing the virus's ability to infect host cells. Research in this area has gained significant traction due to the emergence of various viral infections, prompting scientists to investigate the structural and functional properties of M1 proteins. Recombinant techniques allow for the production of M1 in controlled conditions, facilitating detailed studies on its interactions with host proteins and immune evasion strategies. This research is essential not only for basic virology but also for the development of vaccines and therapeutics aimed at mitigating viral infections. Understanding M1's role can provide insights into vaccine design, particularly in addressing rapidly evolving viruses. Moreover, exploring M1 protein's potential as a target for antiviral drug development underscores its importance in contemporary virology research, making it a key focus for enhancing public health responses to infectious diseases. As such, M1 recombinant protein studies are vital for advancing our knowledge of virology and immunology, ultimately contributing to global health initiatives.

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