Cat: IPD-X41308

Recombinant Bacillus subtilis eglS Protein ,His

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关键信息

  • 基因名

    eglS

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Carboxymethyl-cellulase;CMCase;Cellulase;Endo-1,4-beta-glucanase

  • 种属

    Bacillus subtilis

  • 表达系统

    E. coli

  • 标签

    N- His & C- V5

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P10475

  • 表达区间

    30-499aa

  • 分子量

    59.7 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

EglS is a crucial protein in the study of microbial interactions and enzyme functionality, particularly within the realms of biotechnology and enzymology. Derived from various microorganisms, EglS exhibits significant endoglucanase activity, breaking down cellulose into smaller sugars, thereby playing a vital role in biomass degradation and biofuel production. The quest to explore and characterize EglS has gained prominence due to the increasing global demand for renewable energy sources and sustainable bioprocesses. Researchers have focused on its recombinant expression to enhance yield, stability, and catalytic efficiency, making it a valuable candidate for industrial applications. Moreover, the genetic engineering of EglS allows for the optimization of its properties, enabling the development of tailor-made enzymes for specific substrate affinities. Understanding the structure-function relationship of EglS through advanced methods such as X-ray crystallography and molecular dynamics simulation further opens avenues for improved industrial enzyme design. The study of EglS not only contributes to fundamental microbiological knowledge but also holds promise for practical applications in renewable energy and waste management. As environmental concerns escalate, the role of EglS in bioprocessing and its potential in converting lignocellulosic materials into valuable resources make it a focal point of current research efforts in the quest for sustainable solutions.

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