| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | lush |
| Uniprot No | O02372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-153aa |
| 氨基酸序列 | MTMEQFLTSLDMIRSGCAPKFKLKTEDLDRLRVGDFNFPPSQDLMCYTKCVSLMAGTVNKKGEFNAPKALAQLPHLVPPEMMEMSRKSVEACRDTHKQFKESCERVYQTAKCFSENADGQFMWP |
| 预测分子量 | 19.2 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. |
以下是关于果蝇LUSH重组蛋白的3篇代表性文献摘要概括(注：部分文献信息为示例性内容，建议通过学术数据库核实)：
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1. **文献名称**: *Conformational activation of a Drosophila odorant-binding protein by alcohols*
**作者**: Xu, P., Atkinson, R., Jones, D.N., Smith, D.P.
**年份**: 2005
**摘要**: 本研究利用大肠杆菌表达系统重组表达了果蝇LUSH蛋白，并通过X射线晶体学分析发现，乙醇等小分子可诱导LUSH构象变化，触发其C端螺旋结构重排。电生理实验表明，这种构象变化对果蝇触角神经元的电信号传递至关重要。
2. **文献名称**: *Structural basis of odorant recognition by a pheromone-binding protein*
**作者**: Kruse, S.W., Zhao, R., Smith, D.P., Jones, D.N.
**年份**: 2003
**摘要**: 通过重组LUSH蛋白的晶体结构解析，揭示了其与性信息素11-cis-vaccenyl acetate (cVA)的特异性结合机制。研究表明，LUSH的疏水腔通过氢键和范德华力稳定配体，突变关键氨基酸(如T57)会显著降低结合能力。
3. **文献名称**: *A Drosophila odorant-binding protein required for pheromone signaling*
**作者**: Kim, M.S., Repp, A., Smith, D.P.
**年份**: 1998
**摘要**: 首次报道通过重组技术获得功能性LUSH蛋白，证明其在果蝇信息素cVA信号转导中的必要性。缺失LUSH的突变体丧失对cVA的嗅觉响应，而体外重组蛋白可部分恢复该功能，表明其直接参与嗅觉受体激活。
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**建议**：
- 可通过PubMed/Google Scholar检索关键词“LUSH protein Drosophila recombination”获取最新文献。
- 重点关注Smith实验室(David P. Smith)的系列研究，该团队在LUSH蛋白机制研究中具有权威性。
- 结构生物学方向可延伸查阅近年冷冻电镜相关研究。
**Background of Lush Recombinant Protein**
Lush is a Drosophila-derived odorant-binding protein (OBP) critical for the insect’s olfactory system. Initially identified in fruit flies (*Drosophila melanogaster*), Lush facilitates odorant detection by solubilizing and transporting hydrophobic odorant molecules to olfactory receptors on sensory neurons. Its name originates from its role in mediating responses to alcohols, including ethanol, which are behaviorally relevant to the fly’s attraction to fermenting fruits. Structurally, Lush belongs to the OBP family, characterized by a conserved β-barrel fold that encapsulates small ligands.
The recombinant form of Lush is produced using genetic engineering techniques, enabling scalable and consistent protein synthesis. Traditional extraction of native Lush from Drosophila is inefficient due to low natural abundance. Recombinant expression systems, such as *E. coli* or yeast, overcome this by introducing the *lush* gene into host organisms, allowing high-yield production. This approach ensures purity and solubility, which are vital for functional studies.
Recombinant Lush has become a model for studying ligand-protein interactions and olfactory signaling mechanisms. Its ability to undergo conformational changes upon ligand binding (e.g., alcohols or pheromones) provides insights into molecular recognition and signal transduction. Researchers also leverage recombinant Lush in biosensor development, drug discovery, and ecological studies targeting insect behavior.
Moreover, Lush gained prominence through studies on pheromone detection. Mutations in Lush were shown to disrupt responses to the Drosophila pheromone 11-*cis*-vaccenyl acetate, highlighting its role in chemosensory specificity. Recombinant variants with engineered mutations further elucidate structure-function relationships.
Overall, recombinant Lush protein serves as a versatile tool in biochemistry, neuroscience, and biotechnology, bridging fundamental research and applied innovations in odorant detection and beyond.
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