Cat: IPD-X41004

Recombinant Drosophila melanogaster RpII215 Protein (Yeast),His

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关键信息

  • 基因名

    RpII215

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    DNA-directed RNA polymerase III largest subunit

  • 种属

    Drosophila melanogaster

  • 表达系统

    Yeast

  • 标签

    N- His

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P04052

  • 表达区间

    1579-1881aa

  • 分子量

    33.6 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

RpII215, a vital component of the RNA polymerase II complex, plays a crucial role in the transcription process, influencing gene expression and, consequently, cellular functions. The study of RpII215 is imperative because of its involvement in various biological processes including cell differentiation, proliferation, and response to environmental signals. Researchers are particularly interested in its structure-function relationships, as mutations or dysregulation in RpII215 have been linked to various diseases, including cancer. Understanding the molecular mechanisms by which RpII215 operates could unveil potential therapeutic targets for these conditions. Moreover, advancements in recombinant protein technology have facilitated the production and purification of RpII215, allowing for in-depth functional assays and structural analysis. This research not only enhances our comprehension of the fundamental principles of transcription regulation but also opens avenues for biotechnological applications, such as the development of novel inhibitors or drugs that could modulate the activity of RNA polymerase II in disease contexts. The ongoing investigation into RpII215 thus represents a significant intersection of molecular biology, biochemistry, and clinical research, aiming to decipher the complexities of eukaryotic gene expression and its implications for health and disease.

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