| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RHO |
| Uniprot No | P08134 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-190aa |
| 氨基酸序列 | MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC |
| 预测分子量 | 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RHO重组蛋白的参考文献示例(注：以下文献为示例性内容，非真实存在，仅供格式参考)：
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1. **文献名称**: "Expression and Purification of Functional Recombinant Rhodopsin in Insect Cells"
**作者**: Zhang Y, et al.
**摘要**: 本研究利用杆状病毒-昆虫细胞表达系统成功表达了人源视紫红质(RHO)重组蛋白，并通过亲和层析纯化获得高纯度蛋白。实验验证了重组RHO的光敏特性及与G蛋白的相互作用，为光信号转导机制研究提供工具。
2. **文献名称**: "Crystallographic Analysis of Recombinant RhoA GTPase in the Active Conformation"
**作者**: Tanaka K, et al.
**摘要**: 报道了在大肠杆菌中高效表达并结晶RhoA GTPase重组蛋白的方法，通过X射线衍射解析其活性构象结构，揭示了RhoA与效应蛋白结合的分子机制。
3. **文献名称**: "Optimizing Recombinant Rhodopsin Stability for Biotechnological Applications"
**作者**: Müller S, et al.
**摘要**: 通过定向进化和化学修饰策略，改善了重组视紫红质(RHO)的热稳定性及耐储存性，拓展了其在光遗传学和生物传感器领域的应用潜力。
4. **文献名称**: "Functional Characterization of RHO Mutants in Retinal Degeneration Models"
**作者**: Chen L, et al.
**摘要**: 利用哺乳动物细胞表达系统生成多种RHO突变体重组蛋白，结合体外活性检测和斑马鱼模型，揭示了特定突变导致视网膜色素变性的分子病理机制。
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**建议**：如需真实文献，可通过PubMed、Web of Science等学术平台，以关键词“recombinant rhodopsin”“Rho GTPase expression”“RHO protein purification”等进行检索，并筛选近五年高被引研究。
Rhodopsin (RHO), a light-sensitive G protein-coupled receptor (GPCR), plays a central role in vertebrate vision. Predominantly located in the rod cells of the retina, RHO consists of an opsin protein covalently bound to the chromophore 11-cis-retinal. Upon photon absorption, the chromophore isomerizes to all-trans-retinal, triggering conformational changes in the opsin structure. This activates the associated G-protein transducin, initiating a phototransduction cascade that converts light into electrical signals for the brain. As a prototypical GPCR, RHO's seven-transmembrane helical architecture and signaling mechanisms have become a model for studying GPCR biology.
Recombinant RHO is produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells) for structural and functional studies. Its recombinant form enables detailed investigations into phototransduction abnormalities linked to inherited retinal diseases, such as retinitis pigmentosa (RP) and congenital stationary night blindness. Over 150 RHO mutations are associated with RP, making recombinant variants critical for studying disease mechanisms and evaluating gene therapy strategies, including adeno-associated virus (AAV)-mediated gene replacement.
In structural biology, recombinant RHO has facilitated breakthroughs in understanding GPCR activation dynamics through X-ray crystallography and cryo-EM. Engineered RHO variants also serve as optogenetic tools to control neuronal activity. Despite challenges in maintaining proper folding and post-translational modifications during recombinant production, advances in cell-free systems and lipid nanodiscs have improved functional yield. Ongoing research focuses on stabilizing RHO conformations for drug discovery and developing mutation-agnostic therapies for retinal degeneration. As both a therapeutic target and a molecular tool, recombinant RHO remains pivotal in bridging basic research and clinical innovation.
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