Cat: IPD-X39824

Recombinant Human GLA Protein ,His

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  • 规格
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关键信息

  • 基因名

    GLA

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Alpha-D-galactosidase AAlpha-D-galactoside galactohydrolase;MelibiaseINN: Agalsidase

  • 种属

    Human

  • 表达系统

    E. coli

  • 标签

    N- His

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P06280

  • 表达区间

    32-429aa

  • 分子量

    49.4 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

GLA, or galactosylceramidase, is an essential enzyme involved in the metabolism of complex lipids, specifically sphingolipids. Deficiencies in GLA lead to a rare lysosomal storage disorder known as Krabbe disease, which is characterized by severe neurological impairment and early mortality. The need for effective therapeutic interventions has spurred extensive research into the recombinant production of GLA, which can potentially provide a viable treatment option through enzyme replacement therapy (ERT). Advances in recombinant DNA technology have facilitated the expression of human GLA in various systems, enabling the generation of biologically active enzyme for clinical application. Moreover, understanding the structure and function of GLA at the molecular level has been crucial for developing strategies to enhance its stability and efficacy. Additionally, studies focusing on the localization and delivery methods of GLA within the body aim to optimize its therapeutic potential. The ongoing exploration of GLA reconstitution not only holds promise for patients with Krabbe disease but also paves the way for novel approaches in treating other lysosomal storage disorders. As research progresses, the insights gained from GLA studies could lead to advancements in gene therapy and personalized medicine, offering hope for better management of these debilitating conditions.

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