Cat: PA2000-4237

Recombinant E.coli 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

    eglS;bglC;gld;Endoglucanase

  • 种属

    E.coli

  • 表达系统

    E. coli

  • 标签

    His tag N-Terminus

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P10475

  • 表达区间

    30-499aa

  • 氨基酸序列

    AGTKTPVAKNGQLSIKGTQLVNRDGKAVQLKGISSHGLQWYGEYVNKDSLKWLRDDWGITVFRAAMYTADGGYIDNPSVKNKVKEAVEAAKELGIYVIIDWHILNDGNPNQNKEKAKEFFKEMSSLYGNTPNVIYEIANEPNGDVNWKRDIKPYAEEVISVIRKNDPDNIIIVGTGTWSQDVNDAADDQLKDANVMYALHFYAGTHGQFLRDKANYALSKGAPIFVTEWGTSDASGNGGVFLDQSREWLKYLDSKTISWVNWNLSDKQESSSALKPGASKTGGWRLSDLSASGTFVRENILGTKDSTKDIPETPSKDKPTQENGISVQYRAGDGSMNSNQIRPQLQIKNNGNTTVDLKDVTARYWYKAKNKGQNFDCDYAQIGCGNVTHKFVTLHKPKQGADTYLELGFKNGTLAPGASTGNIQLRLHNDDWSNYAQSGDYSFFKSNTFKTTKKITLYDQGKLIWGTEPN

  • 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, an extracellular glycoside hydrolase, has garnered significant interest in biochemical and industrial research due to its role in the breakdown of complex carbohydrates. This enzyme is primarily derived from bacteria and is known for its ability to hydrolyze glycosidic bonds, facilitating the conversion of polysaccharides into simpler sugars. The study of EglS recombinant protein is essential for several reasons. Firstly, its applications in biotechnology, particularly in biofuel production and food industry processes, make it a valuable candidate for enzymatic research. Secondly, understanding the structure-function relationship of EglS can provide insights into its catalytic mechanism, which is crucial for optimizing its activity and stability under industrial conditions. Recombinant DNA technology allows for the expression of EglS in host organisms, enabling the production of large quantities of the enzyme for detailed functional assays and characterization. Furthermore, the modification of EglS through techniques such as site-directed mutagenesis can enhance its properties, making it more efficient for specific applications. Overall, the research on EglS recombinant protein not only contributes to fundamental enzymology but also has practical implications in various fields, including renewable energy, waste management, and the development of novel food processing techniques.

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