Cat: PA2000-4798

Recombinant Human ddl Protein,His

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关键信息

  • 基因名

    ddl

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    ddl;FHA domain-containing Protein DDL

  • 种属

    Human

  • 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

    P63891

  • 表达区间

    1-356aa

  • 氨基酸序列

    MTKENICIVFGGKSAEHEVSILTAQNVLNAIDKDKYHVDIIYITNDGDWRKQNNITAEIKSTDELHLENGEALEISQLLKESSSGQPYDAVFPLLHGPNGEDGTIQGLFEVLDVPYVGNGVLSAASSMDKLVMKQLFEHRGLPQLPYISFLRSEYEKYEHNILKLVNDKLNYPVFVKPANLGSSVGISKCNNEAELKEGIKEAFQFDRKLVIEQGVNAREIEVAVLGNDYPEATWPGEVVKDVAFYDYKSKYKDGKVQLQIPADLDEDVQLTLRNMALEAFKATDCSGLVRADFFVTEDNQIYINETNAMPGFTAFSMYPKLWENMGLSYPELITKLIELAKERHQDKQKNKYKID

  • 分子量

    47.7 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

Ddl (D-alanyl-D-alanine ligase) is an essential enzyme involved in the biosynthesis of bacterial cell wall peptidoglycan. It catalyzes the formation of D-alanyl-D-alanine dipeptide, a critical building block for bacterial cell wall structure and integrity. Research on Ddl and its related protein structures has gained significant attention due to the rise of antibiotic-resistant bacteria, which threaten global health. Understanding the mechanisms of Ddl and its enzymatic action could provide insights into novel antibacterial strategies. The study of Ddl's protein structure and function is particularly crucial as it may enable the development of new antibiotic agents targeting this enzyme, offering a promising avenue for overcoming resistance. Furthermore, the structural characterization of Ddl can unveil the intricacies of its catalytic mechanism and provide a framework for designing inhibitors. Advances in techniques such as X-ray crystallography and cryo-electron microscopy have enhanced our understanding of Ddl and its interactions with other cellular components. As the global challenge of antibiotic resistance escalates, concerted research efforts focusing on Ddl and similar enzymes are pivotal for enhancing our arsenal against pathogenic bacteria.

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