Cat: IPD-X40157

Recombinant Triticum aestivum MM Protein ,His & SUMO

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关键信息

  • 基因名

    MM

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Prolamin

  • 种属

    Triticum aestivum

  • 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

    P18573

  • 表达区间

    21-307aa

  • 分子量

    49.3 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

MM (Mucolipidosis type II) is a genetic disorder characterized by the accumulation of lysosomal substrates, leading to various health complications. The underlying cause of this condition is often linked to mutations in the GNPTAB gene, which encodes a precursor protein essential for the proper functioning of the enzyme responsible for tagging lysosomal enzymes for degradation. Research into MM recombinant proteins has gained significant attention as a potential therapeutic strategy. Specifically, the production of recombinant forms of the enzyme can aid in the restoration of enzymatic activity, enabling the clearance of accumulated substrates within lysosomes. Advances in genetic engineering techniques have facilitated the development of sophisticated recombinant protein systems that can mimic or enhance natural enzyme function. Studies have focused on optimizing expression systems, improving protein stability, and enhancing delivery methods to target affected tissues more effectively. Moreover, understanding the precise molecular mechanisms involved in MM has opened avenues for exploring gene therapy approaches and other innovative treatments. Overall, the study of MM recombinant proteins not only aims to develop effective interventions for this debilitating condition but also contributes to the broader understanding of lysosomal storage disorders and their management.

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