| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | aroE |
| Uniprot No | P74591 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-290aa |
| 氨基酸序列 | MPSITGKTKL LGVIGYPVGH SLSPVMHNAA LQAMASDYAY VAFPIAPEDL TIAIAGLGAS GVQGLSVTIP HKQVVMPLLT QITETARQVG AVNTLWRDGH GWQGTNTDVE GFLAPLLELK QDWSGRTAVI LGYGGAARAV VVGLTQLGCP EIIVVGRSQE KLAQFANSWT DPKIKQALQV LPWEALSTVI PKASLLINST PVGMAPHPKQ SPLDQSLVEK LPPTAIAYDL IYTPRPTRFL QHAQERGLVT IDGAEMLVQQ GAAALKIWLQ QEVPVDVMRQ ALLHHLEKSA |
| 预测分子量 | 31 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3篇关于aroE重组蛋白的参考文献摘要概括：
1. **标题**：Cloning and expression of the aroE gene encoding shikimate dehydrogenase in *Escherichia coli*
**作者**：Smith J, et al.
**摘要**：研究报道了从大肠杆菌中克隆aroE基因，并通过重组表达系统高效表达具有活性的脱氢酶，优化了纯化条件并验证了其催化功能。
2. **标题**：Characterization of recombinant AroE protein in the shikimate pathway of *Bacillus subtilis*
**作者**：Li X, Wang Y.
**摘要**：通过构建重组质粒在枯草芽孢杆菌中表达AroE蛋白，分析其酶学性质及在芳香族氨基酸合成途径中的调控作用。
3. **标题**：Functional and structural analysis of aroE-encoded shikimate dehydrogenase using recombinant protein technology
**作者**：Garcia-Ramos M, et al.
**摘要**：利用重组蛋白技术获得高纯度AroE脱氢酶，结合晶体结构解析揭示了其底物结合位点，为开发抗菌药物靶点提供依据。
备注：以上文献信息为示例，实际文献需通过学术数据库检索确认。
AroE, encoded by the *aroE* gene, is a critical enzyme in the shikimate pathway, a metabolic route essential for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) in bacteria, plants, and some microorganisms. This pathway is absent in humans, making it an attractive target for antimicrobial drug development. AroE specifically catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, a key intermediate in the pathway. Due to its central role in microbial survival, AroE has been studied extensively for its structural and functional properties.
Recombinant AroE protein is produced via genetic engineering, typically by cloning the *aroE* gene into expression vectors (e.g., *E. coli*) to enable large-scale production. This approach allows for high-purity protein yields, facilitating biochemical and structural studies. Recombinant AroE is widely used to investigate enzyme kinetics, inhibitor screening, and mechanisms of antibiotic resistance. For instance, understanding AroE’s active site and substrate interactions aids in designing novel inhibitors targeting pathogenic bacteria, including *Mycobacterium tuberculosis* and *Staphylococcus aureus*.
Additionally, AroE has applications in metabolic engineering. Shikimate, its product, is a precursor for synthesizing antiviral drugs like oseltamivir (Tamiflu). Recombinant AroE can enhance shikimate production in engineered microbial strains, optimizing industrial biosynthesis. Studies also explore its role in plant-pathogen interactions, as disrupting the shikimate pathway could lead to crop protection strategies.
The recombinant protein’s stability, solubility, and activity are often optimized through codon usage adjustment, fusion tags (e.g., His-tag), or chaperone co-expression. Structural analyses, including X-ray crystallography and cryo-EM, rely on recombinant AroE to elucidate conformational dynamics and guide rational drug design. Overall, AroE recombinant protein serves as a vital tool in both basic research and biotechnological innovation, bridging gaps between microbial metabolism and therapeutic development.
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