Cat: IPD-X40822

Recombinant Vaejovis mexicanus smithi KTx Protein (HEK293),His & Myc

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关键信息

  • 基因名

    KTx

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Toxin Vm24 Toxin alpha-KTx 21.1

  • 种属

    Vaejovis mexicanus smithi

  • 表达系统

    HEK293

  • 标签

    N- His & C- Myc

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P0DJ31

  • 表达区间

    1-36aa

  • 分子量

    7.9 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

KTx recombinant proteins are a focus of extensive research due to their potential applications in various fields, including medicine and biotechnology. KTx, or potassium channel toxins, are naturally occurring peptides found in the venom of certain species of spiders and scorpions. These toxins exhibit a high degree of specificity for different types of potassium channels, making them valuable tools for studying ion channel biology and function. The ability to produce KTx proteins through recombinant DNA technology allows researchers to analyze their structure and function in a controlled environment, facilitating insights into their mechanisms of action. Furthermore, the specific interactions between KTx toxins and potassium channels can aid in the development of novel therapeutics for conditions related to ion channel dysfunction, such as cardiac arrhythmias or neurological disorders. Additionally, understanding the evolutionary adaptations of these proteins can contribute to the field of drug design by identifying lead compounds for pharmaceutical development. As a result, the exploration of KTx recombinant proteins not only enhances our fundamental knowledge of cell physiology but also holds promise for advancing medical science and developing innovative therapies.

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