| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERb |
| Uniprot No | P04626 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 720-976aa |
| 氨基酸序列 | LRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEF |
| 预测分子量 | 36.6 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ERβ(雌激素受体β)重组蛋白的3篇代表性文献示例，涵盖其表达、结构及功能研究：
1. **文献名称**：*"Expression and Purification of Recombinant Human Estrogen Receptor β Ligand-Binding Domain in Escherichia coli"*
**作者**：Smith J, et al.
**摘要**：本研究报道了在大肠杆菌中高效表达人ERβ配体结合域(LBD)的重组蛋白，并通过亲和层析纯化获得高纯度蛋白。作者验证了该重组蛋白与雌激素类似物的结合活性，证实其可用于体外药物筛选。
2. **文献名称**：*"Structural Insights into ERβ Activation Using a Mammalian Cell Expression System"*
**作者**：Zhang L, et al.
**摘要**：通过哺乳动物细胞(HEK293)表达系统制备全长ERβ重组蛋白，结合X射线晶体学解析了其与选择性激动剂的复合物结构，揭示了ERβ特异性激活的分子机制。
3. **文献名称**：*"Functional Characterization of Recombinant ERβ in Drosophila S2 Cells: Implications for Receptor Dimerization"*
**作者**：Tanaka K, et al.
**摘要**：利用果蝇S2昆虫细胞系统表达ERβ重组蛋白，研究其与ERα的异源二聚化能力及转录激活功能，发现ERβ二聚化对特定基因调控通路具有选择性作用。
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**备注**：以上文献为示例性质，实际研究中建议通过PubMed或Web of Science以关键词“recombinant ERβ protein”或“estrogen receptor beta expression”检索最新文献。经典研究可参考Kuiper GG等(1997)关于ERβ克隆与早期功能分析的论文。
**Background of ERβ Recombinant Protein**
Estrogen receptor beta (ERβ) is a member of the nuclear receptor superfamily, playing a critical role in mediating estrogen signaling alongside its isoform ERα. Discovered in 1996. ERβ shares structural homology with ERα, including a DNA-binding domain (DBD) and a ligand-binding domain (LBD), but exhibits distinct tissue distribution and functional roles. ERβ is predominantly expressed in the central nervous system, cardiovascular tissues, immune cells, and reproductive organs, influencing processes such as cell proliferation, apoptosis, and inflammation. Its differential expression and activity compared to ERα have spurred interest in understanding its unique physiological and pathological roles, particularly in hormone-dependent cancers, osteoporosis, and neurodegenerative diseases.
Recombinant ERβ protein is engineered through molecular cloning and expression systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale production for research and therapeutic applications. The recombinant form retains functional domains, allowing studies on ligand-receptor interactions, structural biology, and drug screening. Researchers utilize ERβ recombinant protein to develop selective estrogen receptor modulators (SERMs) or degraders (SERDs), aiming to target ERβ-specific pathways while minimizing off-target effects associated with ERα.
Advances in protein engineering, such as codon optimization and fusion tags, have improved solubility and stability, facilitating crystallography and high-throughput assays. ERβ recombinant tools also aid in producing antibodies for diagnostics and exploring cross-talk with other signaling pathways (e.g., NF-κB or MAPK). Despite progress, challenges remain, including maintaining post-translational modifications in heterologous systems and addressing species-specific functional variations.
Overall, ERβ recombinant protein serves as a vital resource for unraveling estrogen signaling complexity and advancing targeted therapies for conditions like breast cancer, metabolic disorders, and neurological diseases.
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