Cat: IPD-X28501

Recombinant Human THRB Protein,His & SUMO

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Analytical Data

  • Gene name

    THRB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Nuclear receptor subfamily 1 group A member 2c-erbA-2c-erbA-beta

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10828

  • Expression Region

    1-461aa

  • Molecular Weight

    68.8 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

THRB, or thyroid hormone receptor beta, is a crucial protein that mediates the physiological effects of thyroid hormones, which are essential for growth, development, and metabolism in vertebrates. Abnormalities or mutations in THRB can lead to various diseases, including resistance to thyroid hormone disorders and certain types of cancers. Recent research has focused on understanding the structure and function of the THRB protein to unravel its role in gene expression and metabolic regulation. The study of recombinant THRB has gained traction, as it allows for the production of sufficient quantities of the protein for functional assays and structural analysis. This approach facilitates the exploration of THRB's interaction with thyroid hormones and co-regulators, providing insights into its signaling pathways. Additionally, recombinant THRB serves as a valuable tool for drug discovery, enabling the identification of potential therapeutic agents that can modulate its activity. Overall, the ongoing research on THRB recombinant proteins not only enhances our understanding of thyroid hormone signaling but also opens avenues for developing strategies to address thyroid-related disorders and improve health outcomes.

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