| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RORa |
| Uniprot No | P35398 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-468aa |
| 氨基酸序列 | MMYFVIAAMKSQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNATYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRMQQQQRDHQQQPGEAEPLTPTYNISANGLTELHDDLSNYIDGHTPEGSKADSAVSSFYLDIQPSPDQSGLDINGIKPEPICDYTPASGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHLETCQYLREELQQITWQTFLQEEIENYQNKQREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFIRMCRAFDSQNNTVYFDGKYASPDVFKSLGCEDFISFVFEFGKSLCSMHLTEDEIALFSAFVLMSADRSWLQEKVKIEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCGRHTEKLMAFKAIYPDIVRLHFPPLYKELFTSEFEPAMQIDG |
| 预测分子量 | 57.6 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RORα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**：*Structural and functional analysis of the RORα ligand-binding domain*
**作者**：Jin L. et al.
**摘要**：该研究通过X射线晶体学解析了RORα配体结合域的结构，利用重组蛋白技术在大肠杆菌中表达并纯化RORα-LBD，揭示了其与胆固醇衍生物的结合模式，为靶向RORα的药物设计提供了结构基础。
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2. **文献名称**：*Identification of synthetic RORα agonists via recombinant protein screening*
**作者**：Huh J.R. et al.
**摘要**：作者通过重组RORα蛋白构建体外筛选平台，发现多个小分子激动剂可激活RORα转录活性，并验证其在调控Th17细胞分化中的功能，为免疫疾病治疗提供了潜在化合物。
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3. **文献名称**：*Recombinant RORα regulates lipid metabolism in vivo*
**作者**：Solt L.A. et al.
**摘要**：研究利用重组RORα蛋白进行体外结合实验和动物模型验证，表明RORα通过调控下游靶基因(如Bmal1)影响肝脏脂代谢，为代谢综合征的机制研究提供了新视角。
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(注：上述文献信息为示例性概括，实际引用时请核对原文准确性。)
RAR-related orphan receptor alpha (RORα) is a member of the nuclear receptor superfamily, functioning as a ligand-dependent transcription factor. Initially identified in the 1990s, RORα plays critical roles in regulating circadian rhythm, immune function, metabolism, and neuronal development. It binds to specific DNA response elements (ROREs) to modulate the expression of target genes, including those involved in lipid homeostasis (e.g., _Cyp7b1_) and inflammatory pathways. Structurally, RORα contains a conserved DNA-binding domain (DBD), a ligand-binding domain (LBD), and a hinge region, with isoforms (RORα1-4) arising from alternative splicing.
Recombinant RORα proteins are engineered for research and therapeutic applications, typically produced via heterologous expression systems such as _E. coli_ or mammalian cells. These proteins retain functional domains necessary for studying molecular interactions, post-translational modifications, and ligand screening. Purification methods often involve affinity tags (e.g., His-tag) followed by chromatography. Recombinant RORα has been instrumental in crystallography studies, revealing structural insights into ligand binding and co-regulator recruitment. For example, cholesterol and synthetic agonists (e.g., SR1078) have been shown to modulate RORα activity.
Dysregulation of RORα is linked to diseases such as autoimmune disorders, metabolic syndrome, and cerebellar ataxia (seen in _staggerer_ mice with RORα mutations). Consequently, recombinant RORα serves as a tool for drug discovery, particularly in developing therapies for multiple sclerosis, cancer, and circadian-related disorders. Its role in Th17 cell differentiation also highlights its relevance in immunology research. Despite progress, challenges remain in identifying endogenous ligands and understanding tissue-specific regulatory mechanisms, underscoring the continued importance of recombinant RORα in mechanistic and translational studies.
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