Cat: IPD-X41135

Recombinant Human herpesvirus 6B KA3L Protein ,His & Myc

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Analytical Data

  • Gene name

    KA3L

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    /

  • Species

    Human herpesvirus 6B

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P52539

  • Expression Region

    135-364aa

  • Molecular Weight

    34.6 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

KA3L recombinant protein is an emerging area of interest in molecular biology and protein engineering, primarily due to its potential applications in therapeutic development and biotechnological innovations. KA3L is a fusion protein that combines elements from different functional domains, creating a chimera with enhanced biological properties. The unique structure of KA3L allows it to demonstrate improved stability, solubility, and binding affinity to specific targets, making it a valuable candidate for drug delivery systems and targeted therapies. Additionally, the ongoing research into its mechanism of action provides insights into protein interactions and signaling pathways that could pave the way for novel treatments in various medical conditions. The ability to produce KA3L in recombinant systems facilitates large-scale production and purifies the protein for further investigations, thus playing a crucial role in advancing our understanding of protein function. As such, the study of KA3L recombinant protein is positioned at the intersection of biochemistry, molecular biology, and therapeutic development, highlighting its significance in both academic research and industrial applications.

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