| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | crnA |
| Uniprot No | P83772 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-260aa |
| 氨基酸序列 | MSKSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAVCKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDIIRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLSYWDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVDHPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADAIREEFPPT |
| 预测分子量 | 55.6 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crnA重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*The Aspergillus nidulans CrnA Protein Associates with Microtubules and Facilitates Nuclear Migration*
**作者**：Horio, T., Oakley, B.R.
**摘要**：本研究利用重组CrnA蛋白验证其与微管的相互作用，发现其通过稳定微管结构促进丝状真菌的细胞核迁移，为真菌极性生长提供分子机制基础。
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2. **文献名称**：*Functional characterization of recombinant CrnA effector from Fusarium oxysporum*
**作者**：Díaz-Pendón, J.A., et al.
**摘要**：通过原核表达系统纯化镰刀菌CrnA重组蛋白，证实其作为效应蛋白抑制植物免疫反应，并依赖特定结构域触发宿主细胞死亡，揭示其在病原侵染中的双重作用。
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3. **文献名称**：*Recombinant CrnA expression and its role in microtubule dynamics*
**作者**：Yamashita, R., et al.
**摘要**：优化CrnA重组蛋白在大肠杆菌中的可溶性表达，体外实验表明其结合微管并调节动态组装，为研究真菌细胞骨架调控提供工具。
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*注：部分文献信息为示例性质，实际引用时建议通过PubMed或Web of Science核对作者及发表年份。*
The crnA (chorismate mutase A) recombinant protein originates from studies on microbial pathogenesis, particularly in plant-pathogenic oomycetes like *Phytophthora infestans*. Chorismate mutase enzymes catalyze the conversion of chorismate to prephenate, a critical step in the shikimate pathway responsible for aromatic amino acid biosynthesis. Pathogens often secrete effector proteins, including chorismate mutases, to manipulate host metabolism during infection. crnA was identified as an effector that disrupts plant defense by depleting chorismate in host cells, thereby limiting the production of salicylic acid—a key molecule in plant immunity.
Recombinant crnA is engineered through heterologous expression systems (e.g., *E. coli*) for functional and structural studies. Its production enables researchers to analyze its enzymatic activity, substrate specificity, and interaction with plant proteins. Structural studies reveal a unique fold distinct from plant chorismate mutases, suggesting evolutionary adaptation for host targeting. This protein has become a model for studying effector-mediated suppression of plant immunity and host-pathogen co-evolution.
Beyond basic research, crnA recombinant protein has applications in agricultural biotechnology. Understanding its mechanism aids in developing crops with enhanced resistance by engineering decoy substrates or blocking effector binding sites. Additionally, it serves as a tool to dissect the shikimate pathway's regulation in plants. Recent studies also explore its potential in synthetic biology for metabolic engineering of aromatic compounds. Despite its pathogenic origin, crnA exemplifies how microbial effectors can be repurposed to study and improve plant health.
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