| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | aroA |
| Uniprot No | P0A6D4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-427aa |
| 氨基酸序列 | MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA |
| 预测分子量 | 53.5 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aroA重组蛋白的模拟参考文献示例(注：以下内容为示例，实际文献需通过学术数据库查询)：
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1. **《Expression and purification of recombinant aroA protein from Salmonella typhimurium》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌表达系统克隆并纯化了沙门氏菌来源的aroA基因编码的EPSP合成酶，验证了其酶活性，并分析了重组蛋白在体外催化莽草酸途径的功能。
2. **《Structural insights into glyphosate resistance via aroA mutation in transgenic crops》**
- 作者：Wang L, et al.
- 摘要：解析了抗草甘膦作物中突变型aroA重组蛋白的晶体结构，揭示了关键氨基酸替换如何降低草甘膦与EPSP合成酶的结合能力，从而赋予植物抗性。
3. **《Functional characterization of aroA-deficient E. coli complemented with plant-derived recombinant enzyme》**
- 作者：Chen R, et al.
- 摘要：通过植物来源的aroA重组蛋白回补大肠杆菌突变株，证明了该蛋白在芳香族氨基酸合成中的功能保守性，并评估了其在不同pH条件下的稳定性。
4. **《High-level production of aroA recombinant protein in Pichia pastoris for herbicide resistance screening》**
- 作者：Garcia M, et al.
- 摘要：利用毕赤酵母系统高效表达aroA重组蛋白，优化发酵工艺后获得高纯度产物，并用于高通量筛选新型除草剂抑制剂。
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如需真实文献，建议在PubMed、Web of Science或Google Scholar中检索关键词“aroA recombinant protein”“EPSP synthase expression”或“glyphosate resistance aroA”。
The aroA gene encodes 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), a critical enzyme in the shikimate pathway responsible for aromatic amino acid biosynthesis in plants, bacteria, and fungi. This pathway is absent in animals, making EPSPS an attractive target for antimicrobials and herbicides. Recombinant aroA proteins are genetically engineered versions of EPSPS produced in heterologous expression systems (e.g., E. coli) for research and industrial applications.
Interest in aroA stems from its role in glyphosate resistance. Glyphosate, a broad-spectrum herbicide, inhibits EPSPS by mimicking its substrate PEP. Naturally occurring or lab-engineered aroA variants with reduced glyphosate binding have been pivotal in developing herbicide-resistant crops (e.g., Roundup Ready varieties). Recombinant aroA proteins enable detailed studies of resistance mechanisms through structural analysis, enzyme kinetics, and mutagenesis experiments.
In biotechnology, aroA recombinant proteins serve as tools to optimize microbial production of aromatic compounds (e.g., precursors for pharmaceuticals). Modified aroA pathways in engineered strains can enhance yields of shikimate-derived products like L-DOPA or vanillin.
Additionally, bacterial aroA has been explored as a target for novel antibiotics, given its essentiality in pathogenic microbes. Recombinant EPSPS proteins facilitate high-throughput screening of inhibitors and vaccine development studies, particularly for gram-negative pathogens where aroA mutations may attenuate virulence.
The production of recombinant aroA typically involves codon optimization, affinity tagging, and purification via chromatography. Challenges include maintaining enzymatic activity post-purification and minimizing host toxicity during expression. Recent advances in protein engineering and structural biology continue to expand its applications in agriculture, medicine, and industrial biotechnology.
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