| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | aroD |
| Uniprot No | P24670 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252aa |
| 氨基酸序列 | MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREATFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFTFRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTGDADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVLRLRKMQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPVITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVNDLRSVLMILHNA |
| 预测分子量 | 29.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于aroD重组蛋白的虚构参考文献示例(内容为模拟创作，非真实文献)：
1. **标题**：Cloning and Functional Characterization of the aroD Gene in Escherichia coli
**作者**：Smith J, et al.
**摘要**：研究报道了aroD基因的克隆及在大肠杆菌中的重组表达，证实其编码的3-脱氢奎宁酸脱水酶在细菌芳香族氨基酸合成中的关键作用，并优化了重组蛋白的纯化流程。
2. **标题**：Development of a Salmonella Vaccine Using Recombinant aroD Protein as Antigen
**作者**：Zhang L, et al.
**摘要**：通过敲除沙门氏菌aroD基因并表达重组aroD蛋白，评估其作为减毒活疫苗抗原的潜力，实验证明该蛋白能诱导小鼠产生保护性免疫应答。
3. **标题**：Structural Analysis of aroD-Encoded Enzyme in Mycobacterium tuberculosis
**作者**：Johnson R, et al.
**摘要**：利用X射线晶体学解析结核分枝杆菌aroD重组蛋白的三维结构，揭示了其底物结合位点特征，为针对该酶的抗菌药物设计提供结构基础。
4. **标题**：Metabolic Engineering of Yeast via aroD Overexpression for Shikimate Pathway Optimization
**作者**：Yamamoto K, et al.
**摘要**：通过在酿酒酵母中过表达重组aroD蛋白，显著提升莽草酸途径代谢通量，为微生物合成芳香族化合物提供高效工程菌株构建策略。
**Background of aroD Recombinant Protein**
The *aroD* gene encodes 3-dehydroquinate dehydratase (DHQ dehydratase), a key enzyme in the shikimate pathway, a metabolic route essential for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) in bacteria, fungi, and plants. This pathway is absent in mammals, making it a promising target for antimicrobial drug development. The *aroD*-encoded enzyme catalyzes the third step of the shikimate pathway, converting 3-dehydroquinate to 3-dehydroshikimate. Disruption of *aroD* leads to auxotrophy for aromatic compounds, limiting bacterial growth in environments lacking these nutrients.
Recombinant aroD protein is produced via genetic engineering, often using heterologous expression systems like *Escherichia coli*. Its production enables functional and structural studies to elucidate catalytic mechanisms, substrate specificity, and potential inhibition strategies. Due to its role in pathogen viability, aroD is explored as a target for novel antibiotics, particularly against multidrug-resistant strains. For example, *aroD*-deficient attenuated pathogens (e.g., *Salmonella* Typhi) have been investigated as live vaccines, as they require supplemented aromatic compounds to proliferate, ensuring limited persistence in hosts.
Additionally, recombinant aroD serves as a tool in metabolic engineering to optimize microbial production of aromatic compounds for industrial applications. Studies on its enzymatic activity and regulation also contribute to understanding evolutionary conservation across species and resistance mechanisms. Overall, aroD recombinant protein bridges fundamental research and applied biotechnology, offering insights into antimicrobial development, vaccine design, and synthetic biology.
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