Cat: PA2000-904DB

Recombinant Human AVPI1 Protein,His

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Analytical Data

  • Gene name

    AVPI1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    AVPI1;Arginine vasopressin-induced Protein 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q5T686

  • Expression Region

    1-147aa

  • AA Sequence

    MGTPASVVSE PPPWQAPIEA RGRKQASANI FQDAELLQIQ ALFQRSGDQL AEERAQIIWE CAGDHRVAEA LKRLRRKRPP RQKPLGHSLH HCSRLRILEP HSALANPQSA TETASSEQYL HSRKKSARIR RNWRKSGPTS YLHQIRH

  • Molecular Weight

    16.7 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

AVPI1, a member of the antiviral protein family, has garnered attention for its role in mediating plant defense mechanisms against a variety of pathogenic viruses. As agricultural sustainability becomes increasingly vital, understanding the function and regulation of such proteins is essential for developing resilient crop varieties. AVPI1's mechanism involves the recognition of viral genetic material, triggering defense responses that limit viral replication and spread. Recent studies have employed molecular biology techniques to characterize AVPI1's structure and function, revealing its potential as a biotechnological tool for enhancing resistance in economically important crops. Additionally, the implications of AVPI1 in cross-kingdom immunity highlight its significance beyond plant systems, indicating a broader potential application in combating viral infections. As research continues to elucidate the pathways and interactions involved, AVPI1 stands as a promising candidate for genetic engineering approaches aimed at improving agricultural resilience in the face of emerging viral threats.

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