Cat: IPD-X25331

Recombinant Cynomolgus Transthyretin/TTR Protein (HEK293),His & Myc

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Analytical Data

  • Gene name

    Transthyretin/TTR

  • 简介

    Transthyretin (TTR) is a thyroid hormone-binding protein that may be involved in transporting thyroxine from the blood to the brain. As a homotetramer, TTR forms a dimer of dimers with a ligand-regulated central channel. Transthyretin/TTR Protein, Cynomolgus (HEK293, His, Myc) is the recombinant cynomolgus-derived Transthyretin/TTR protein, expressed by HEK293 , with N-6*His, N-Myc labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured in a cell proliferation assay using A549 cells. The ED50 this effect is 1.794 ng/mL, corresponding to a specific activity is 5.57×105 units/mg. Measured in a cell proliferation assay using A549 cells. The ED50 this effect is 1.794 ng/mL, corresponding to a specific activity is 5.57×105 units/mg.

  • Alternative Names

    TTR; QccE-10711; QccE-14396; Transthyretin; Prealbumin

  • Species

    Cynomolgus

  • Source

    HEK293

  • Tag

    N-6*His;N-Myc

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q8HXW1

  • Expression Region

    G21-E147

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    18 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

Transthyretin (TTR) is a tetrameric protein primarily produced in the liver and is crucial for the transport of thyroxine and retinol-binding protein. It plays a significant role in maintaining thyroid hormone balance and vitamin A metabolism in the human body. However, mutations in the TTR gene can lead to various amyloid diseases, such as familial amyloidotic polyneuropathy and senile systemic amyloidosis, which are characterized by the deposition of misfolded TTR. The study of recombinant TTR proteins has gained momentum due to their potential therapeutic applications, including the development of small molecules that stabilize the tetrameric form of TTR and prevent its misfolding. Moreover, recombinant TTR can be utilized to explore the mechanisms of amyloidogenesis, investigate structure-function relationships, and enhance our understanding of TTR-related pathologies. Current research is focused on elucidating the protein’s folding pathways, identifying stabilizing ligands, and evaluating their implications in drug design. The advancement of recombinant DNA technology has facilitated the expression and purification of TTR in various model systems, enabling high-throughput screening of compounds that may mitigate the aggregation propensity of TTR. With ongoing studies, recombinant TTR represents a promising avenue for effective therapeutic strategies aimed at combating TTR-related diseases and improving patient outcomes.

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