| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NR3C1 |
| Uniprot No | P04150 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 521-777aa |
| 氨基酸序列 | VPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK |
| 预测分子量 | 42.8 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NR3C1重组蛋白的3篇参考文献及其摘要概括：
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1. **"Purification and structural analysis of the human glucocorticoid receptor ligand-binding domain expressed in Escherichia coli"**
*Dahlman-Wright, K., et al. (1995)*
该研究报道了在大肠杆菌中高效表达人源NR3C1(糖皮质激素受体)配体结合域(LBD)的方法，并通过亲和层析和离子交换层析纯化获得高纯度重组蛋白。研究进一步利用圆二色谱和X射线晶体学分析其二级和三级结构，验证了重组蛋白的功能性构象。
2. **"Crystal structure of the glucocorticoid receptor ligand-binding domain reveals a novel mode of receptor dimerization and coactivator recognition"**
*Bledsoe, R.K., et al. (2002)*
本研究解析了人源NR3C1配体结合域与地塞米松复合物的晶体结构(分辨率2.3 Å)，揭示了糖皮质激素受体独特的二聚化模式及其与共激活因子的相互作用机制。重组蛋白在昆虫细胞中表达并通过配体亲和层析纯化，为后续药物设计提供了结构基础。
3. **"Functional characterization of the full-length glucocorticoid receptor expressed in mammalian cells"**
*Kadmiel, M., et al. (2011)*
作者在哺乳动物细胞(HEK293)中表达了全长的NR3C1重组蛋白，并通过荧光素酶报告基因实验验证其转录调控活性。研究还比较了不同表达系统(如原核与真核)对受体功能的影响，强调哺乳动物系统在保留翻译后修饰及配体响应性方面的优势。
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这些文献涵盖了NR3C1重组蛋白的表达系统优化、结构解析及功能研究，为相关领域提供了技术参考和理论支持。如需扩展，可进一步检索近年基于冷冻电镜或药物筛选的研究。
NR3C1 (Nuclear Receptor Subfamily 3 Group C Member 1), also known as the glucocorticoid receptor (GR), is a ligand-activated transcription factor that plays a central role in mediating the physiological effects of glucocorticoids. These steroid hormones, including cortisol in humans, regulate critical processes such as metabolism, immune response, stress adaptation, and inflammation. The NR3C1 protein contains three functional domains: an N-terminal transcriptional activation domain, a central DNA-binding domain, and a C-terminal ligand-binding domain. Upon glucocorticoid binding, NR3C1 undergoes conformational changes, dissociates from chaperone proteins, translocates to the nucleus, and either activates or represses target gene expression by binding to glucocorticoid response elements (GREs) or interacting with other transcription factors.
Recombinant NR3C1 proteins are engineered in vitro using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional GR for research and therapeutic applications. These proteins retain key structural features, enabling studies on glucocorticoid signaling mechanisms, receptor-ligand interactions, and transcriptional regulation. Recombinant variants may include tags (e.g., His-tag, GST-tag) for purification or detection, and mutations to investigate functional domains or disease-associated polymorphisms. They are widely used in biochemical assays (e.g., electrophoretic mobility shift assays), high-throughput drug screening, structural studies (X-ray crystallography), and cell-based models to dissect GR’s role in pathologies like inflammatory diseases, cancer, and metabolic disorders. The production of recombinant NR3C1 has advanced understanding of glucocorticoid resistance mechanisms and the development of selective GR modulators with improved therapeutic profiles.
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