| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | GRa |
| Uniprot No | P13403 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-190aa |
| 氨基酸序列 | AEGGDNQSSAVSDRASLFGLLSGGTGQGLGIGESVDLEMMGNTYRVERPTGNPDLLKIAIKASDGSYSEVGNVNVEEVIDTMKSMQRDEDIFLRALNKGETVEEAIEDVAQAEGLNSEQTLQLEDAVSAVASVVQDEMKVIDDVQQLEKDKQQLKDDIGFLTGERE |
| 预测分子量 | 19.9 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. |
以下是关于糖皮质激素受体α(GRα)重组蛋白的3篇代表性文献摘要，供参考：
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1. **文献名称**：*Primary structure and expression of a functional human glucocorticoid receptor cDNA*
**作者**：Hollenberg, S.M., et al. (1985)
**摘要**：该研究首次克隆并表达了人源糖皮质激素受体α(GRα)的cDNA，证实其在哺乳动物细胞中的功能活性。重组GRα能够结合地塞米松等配体，并激活下游基因调控，为后续受体结构研究奠定基础。
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2. **文献名称**：*Structure and function of the glucocorticoid receptor ligand binding domain*
**作者**：Rogatsky, I., et al. (2002)
**摘要**：文章通过重组表达GRα的配体结合域(LBD)，结合X射线晶体学解析其三维结构，揭示了地塞米松等糖皮质激素与受体的相互作用机制，阐明了配体诱导构象变化对转录活性的影响。
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3. **文献名称**：*Selective modulation of glucocorticoid receptor activity as a strategy to enhance anti-inflammatory therapy*
**作者**：Lewis-Tuffin, L.J., et al. (2012)
**摘要**：研究利用重组GRα蛋白筛选选择性调节剂，发现部分化合物可分离抗炎与代谢副作用相关的信号通路，为开发靶向GRα的安全型抗炎药物提供了新策略。
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**备注**：若需更近期文献或特定研究方向(如蛋白纯化、疾病模型应用)，建议在PubMed或Web of Science中检索关键词“Glucocorticoid Receptor alpha recombinant”或“GRα protein engineering”。
GRa (Glucocorticoid Receptor alpha) is a critical member of the nuclear receptor superfamily, functioning as a ligand-dependent transcription factor. It mediates the effects of glucocorticoids, steroid hormones essential for regulating metabolism, immune responses, inflammation, and stress adaptation. Upon binding to cortisol or synthetic glucocorticoids like dexamethasone, GRa undergoes conformational changes, translocates to the nucleus, and modulates gene expression by interacting with glucocorticoid response elements (GREs) or tethering to other transcription factors. Dysregulation of GRa signaling is linked to diseases such as Cushing’s syndrome, autoimmune disorders, and cancer, highlighting its therapeutic relevance.
Recombinant GRa proteins are engineered using heterologous expression systems (e.g., bacterial, insect, or mammalian cells) to produce purified, functional receptor variants for research and drug discovery. These proteins retain key domains: a C-terminal ligand-binding domain (LBD) for hormone interaction, a central DNA-binding domain (DBD), and an N-terminal regulatory region. Recombinant GRa enables structural studies (e.g., crystallography, cryo-EM) to resolve mechanisms of ligand binding, coactivator recruitment, and antagonist effects. It also facilitates high-throughput screening for GRa modulators with improved specificity or reduced side effects compared to classical glucocorticoids.
Furthermore, GRa isoforms and mutations associated with glucocorticoid resistance can be studied using recombinant systems to dissect pathological mechanisms. Despite its utility, challenges remain in mimicking post-translational modifications and cellular contexts ex vivo. Overall, recombinant GRa serves as a vital tool for unraveling glucocorticoid signaling complexity and advancing targeted therapies in endocrinology, oncology, and immunology.
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