Cat: IPD-X22735

Recombinant Mouse Transthyretin/TTR Protein,His & SUMO

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关键信息

  • 基因名

    Transthyretin/TTR

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    ATTR Prealbumin; TBPA; PALB;

  • 种属

    Mouse

  • 表达系统

    E. coli

  • 标签

    N- His-SUMO

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P07309

  • 表达区间

    21-147aa

  • 分子量

    26.6 kDa

  • 内毒素

    < 1.0 EU per μg protein as determined by the LAL method.

  • 性状

    Freeze-dried powder

  • 缓冲液

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • 复溶方法

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • 个性化定制

    点位突变 标签定制 buffer定制 全长蛋白定制

  • 稳定性测试

    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.

  • 保存条件 & 期限

    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.

  • 运输条件

    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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背景信息

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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