| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | aro-2 |
| Uniprot No | Q12640 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-432aa |
| 氨基酸序列 | MSTFGHYFRVTTYGESHCKSVGCIVDGVPPGMELTEDDIQPQMTRRRPGQSAITTPRDEKDRVIIQSGTEFGVTLGTPIGMLVMNEDQRPKDYGNKTMDIYPRPSHADWTYLEKYGVKASSGGGRSSARETIGRVAAGAIAEKYLKLAYGVEIVAFVSSVGSEHLFPPTAEHPSPSTNPEFLKLVNSITRETVDSFLPVRCPDAEANKRMEDLITKFRDNHDSIGGTVTCVIRNVPSGLGEPAFDKLEAMLAHAMLSIPATKGFEVGSGFGGCEVPGSIHNDPFVSAENTEIPPSVAASGAARNGIPRPKLTTKTNFSGGIQGGISNGAPIYFRVGFKPAATIGQEQTTATYDGTSEGVLAAKGRHDPSVVPRAVPIVEAMAALVIMDAVLAQQARHTAKSLLPPLKQTINSGKDTVGNGVSENVQESDLAQ |
| 预测分子量 | 46.8 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aro-2重组蛋白的3篇示例参考文献(内容为虚构，仅作格式参考)：
1. **《Functional characterization of recombinant ARO-2 enzyme in aromatic amino acid biosynthesis》**
- 作者：Smith J, et al.
- 摘要：研究在大肠杆菌中表达并纯化重组ARO-2蛋白，证实其作为分支酸合酶(chorismate synthase)的活性，并分析其在苯丙氨酸、酪氨酸生物合成途径中的催化机制。
2. **《Crystal structure of ARO-2 from Saccharomyces cerevisiae: Insights into substrate binding》**
- 作者：Li X, et al.
- 摘要：解析酿酒酵母来源的ARO-2重组蛋白晶体结构，揭示其与底物EPSP的结合模式，为设计芳香族氨基酸合成抑制剂提供结构基础。
3. **《Heterologous expression of aro-2 in Bacillus subtilis for metabolic engineering applications》**
- 作者：Wang Y, et al.
- 摘要：将植物病原菌的aro-2基因重组表达于枯草芽孢杆菌中，优化发酵条件以提高分支酸产量，推动其在合成生物学中的应用。
(注：若需真实文献，请通过PubMed或SciHub检索关键词“ARO2 recombinant protein”或“chorismate synthase heterologous expression”。)
The aro-2 gene encodes a key enzyme in the aromatic amino acid biosynthesis pathway, which is essential for the production of phenylalanine, tyrosine, and tryptophan in microorganisms, plants, and some parasites. In pathogenic organisms like *Plasmodium falciparum* (the malaria parasite), which cannot salvage aromatic amino acids from hosts, the aro-2-encoded enzyme becomes a critical drug target. This pathway is absent in humans, making it a promising focus for antimicrobial or antiparasitic drug development.
The recombinant aro-2 protein is typically produced using heterologous expression systems, such as *E. coli* or yeast, to enable large-scale purification and functional studies. Its structure and enzymatic activity—often involving catalyzing steps like the conversion of 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) to downstream intermediates—have been explored to design inhibitors. For example, glyphosate, a herbicide, targets a related plant aromatic biosynthesis enzyme, highlighting the pathway's vulnerability.
Research on recombinant aro-2 protein aids in understanding resistance mechanisms, optimizing inhibitor specificity, and developing novel therapeutics. In malaria, aro-2-based studies have identified potential compounds that disrupt parasite survival without affecting human cells. Additionally, recombinant aro-2 serves as an antigen in vaccine research to elicit immune responses against parasitic infections.
Overall, aro-2 recombinant protein bridges biochemical research and translational applications, offering insights into metabolic vulnerabilities of pathogens and strategies to combat diseases like malaria, while underscoring the importance of conserved microbial pathways in drug discovery.
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