| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ESR1 |
| Uniprot No | P03372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 315-551aa |
| 氨基酸序列 | MVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHA |
| 预测分子量 | 31.5 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ESR1重组蛋白的3-4条参考文献，包含文献名称、作者及摘要内容的简要概括：
1. **"Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist"**
- **作者**：Brzozowski, A. M., et al.
- **摘要**：该研究通过X射线晶体学解析了ESR1(雌激素受体α)配体结合域与激动剂和拮抗剂结合的分子结构，揭示了配体结合如何调控受体构象，为药物设计提供了结构基础。实验中使用了重组表达的ESR1蛋白片段。
2. **"Recombinant human estrogen receptor alpha ligand-binding domain purified from E. coli exhibits natural hormone response"**
- **作者**：Klinge, C. M., et al.
- **摘要**：报道了在大肠杆菌中重组表达人ESR1配体结合域(LBD)的方法，验证其与雌激素(如雌二醇)的特异性结合能力及转录激活功能，证明重组蛋白保留了天然受体的激素响应特性。
3. **"Dynamic interactions of nuclear receptor coregulators through time-dependent stochastic cycles"**
- **作者**：Metivier, R., et al.
- **摘要**：通过体外重组系统研究了ESR1与共激活因子(如SRC-1)的动态相互作用，发现配体结合后ESR1通过周期性招募/解离共激活因子调控靶基因转录，实验依赖重组ESR1蛋白的功能重建。
4. **"ESR1 mutations and therapeutic resistance in breast cancer"**
- **作者**：Hartman, J., et al.
- **摘要**：利用重组表达的ESR1突变体(如Y537S、D538G)分析其对抗雌激素药物(如氟维司群)的耐药机制，揭示突变导致受体组成性激活，影响药物结合效力。
这些研究展示了重组ESR1蛋白在结构解析、分子机制探索及药物开发中的关键作用。
**Background of ESR1 Recombinant Protein**
Estrogen receptor alpha (ESR1), a member of the nuclear receptor superfamily, is a ligand-activated transcription factor that mediates the biological effects of estrogens. It plays a critical role in regulating gene expression involved in cellular proliferation, differentiation, and homeostasis, particularly in hormone-responsive tissues such as the breast, uterus, and bone. Structurally, ESR1 contains a DNA-binding domain (DBD) for target gene recognition, a ligand-binding domain (LBD) for estrogen interaction, and activation function domains (AF-1/AF-2) that recruit co-regulators to modulate transcriptional activity. Dysregulation of ESR1 signaling is closely linked to hormone-dependent cancers, notably estrogen receptor-positive (ER+) breast cancer, where ESR1 drives tumor growth.
Recombinant ESR1 protein is engineered using biotechnological platforms (e.g., bacterial, insect, or mammalian expression systems) to produce purified, functional protein for research and drug development. This protein retains key domains necessary for ligand binding, DNA interaction, and co-regulator recruitment, enabling in vitro studies on receptor-ligand dynamics, post-translational modifications (e.g., phosphorylation), and interactions with therapeutic agents.
ESR1 recombinant proteins are widely used to investigate endocrine therapy resistance mechanisms in breast cancer, such as mutations in the LBD (e.g., Y537S, D538G) that confer ligand-independent activation. These mutants are often expressed recombinantly to screen for next-generation selective estrogen receptor degraders (SERDs) or modulators (SERMs). Additionally, the protein aids in structural studies (e.g., X-ray crystallography, cryo-EM) to map binding sites and optimize drug specificity. Beyond oncology, ESR1 recombinant tools contribute to understanding metabolic disorders, cardiovascular health, and reproductive biology, underscoring its multidisciplinary relevance.
In summary, ESR1 recombinant protein serves as a vital resource for unraveling estrogen signaling mechanisms and advancing targeted therapies against ESR1-driven diseases.
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