| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERRa |
| Uniprot No | P11474 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 231-330aa |
| 氨基酸序列 | LFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPL QDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLK |
| 预测分子量 | 37 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ERRα重组蛋白的3篇参考文献示例，信息基于领域内常见研究方向整理：
1. **"Production and characterization of recombinant human estrogen-related receptor alpha ligand-binding domain"**
*作者: Greschik H, et al.*
摘要：该研究报道了人源ERRα配体结合域(LBD)在大肠杆菌中的重组表达及纯化，通过X射线晶体学解析其三维结构，分析了受体与共激活因子的相互作用机制。
2. **"Functional analysis of ERRα recombinant protein in mitochondrial biogenesis regulation"**
*作者: Villena JA, et al.*
摘要：利用哺乳动物细胞系统表达ERRα重组蛋白，证实其通过结合靶基因启动子区域(如PGC-1α)调控线粒体生成，并发现特定配体对其转录活性的增强效应。
3. **"Purification and in vitro reconstitution of ERRα transcriptional complex"**
*作者: Zhang Y, et al.*
摘要：开发了基于镍亲和层析的ERRα重组蛋白纯化方案，并证明其在体外可与DNA响应元件特异性结合，为高通量筛选ERRα调节剂提供实验体系。
*注：以上为模拟文献示例，实际文献需通过PubMed/Google Scholar检索关键词“ERRα recombinant protein”或“Estrogen-related receptor alpha expression”获取。建议结合具体研究方向筛选近期高相关论文。*
**Background of ERRa Recombinant Protein**
Estrogen-related receptor alpha (ERRα, NR3B1) is a member of the nuclear receptor superfamily, initially identified for its structural similarity to estrogen receptors (ERs). Despite its classification, ERRα does not bind natural estrogens but functions as a constitutively active transcription factor. It plays a pivotal role in regulating energy metabolism, mitochondrial biogenesis, and cellular adaptation to metabolic stress. ERRα is highly expressed in tissues with high energy demands, such as the heart, skeletal muscle, and liver, where it governs the expression of genes involved in oxidative phosphorylation, fatty acid oxidation, and glucose metabolism.
The recombinant ERRa protein is engineered to study its molecular mechanisms and interactions. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains functional domains critical for DNA binding (DBD) and ligand-independent transcriptional activation (AF-2 domain). Researchers utilize recombinant ERRα to investigate its role in diseases like cancer, metabolic syndromes, and neurodegenerative disorders, where dysregulated ERRα activity is linked to pathological metabolic reprogramming.
ERRα is considered an orphan receptor due to the lack of known endogenous ligands, though synthetic ligands (agonists/antagonists) have been developed. Recombinant protein studies aid in screening these ligands for therapeutic potential. Additionally, structural analyses of recombinant ERRα have provided insights into its interaction with coactivators (e.g., PGC-1α) and DNA response elements. Challenges include maintaining its native conformation *in vitro* and elucidating tissue-specific regulatory networks.
Overall, ERRa recombinant protein serves as a vital tool for deciphering metabolic regulation and developing therapies targeting ERRα-associated pathologies.
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