| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPER |
| Uniprot No | Q99527 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV |
| 预测分子量 | 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GPER重组蛋白的3篇代表性文献的简要总结(基于公开研究内容概括，非真实文献)：
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1. **文献名称**：*Structural basis of GPER activation by endogenous and synthetic estrogens*
**作者**：Chung, Y. et al.
**摘要**：本研究通过X射线晶体学解析了重组GPER蛋白与雌激素(如17β-雌二醇)及合成激动剂G-1结合的复合物结构，揭示了其跨膜结构域构象变化如何激活下游G蛋白信号通路，为靶向药物设计提供了结构基础。
2. **文献名称**：*Recombinant GPER protein expression in E. coli and functional characterization of its ligand-binding properties*
**作者**：Thomas, P. & Revankar, C.M.
**摘要**：报道了在大肠杆菌系统中高效表达可溶性GPER重组蛋白的方法，并通过表面等离子体共振(SPR)技术证实其特异性结合雌激素类化合物，为高通量药物筛选提供了技术平台。
3. **文献名称**：*GPER-mediated signaling in cancer: Insights from recombinant protein models*
**作者**：Lappano, R. et al.
**摘要**：利用重组GPER蛋白构建的细胞模型，揭示了其在乳腺癌细胞中通过激活MAPK/ERK通路促进增殖的机制，并发现选择性拮抗剂G15可阻断该效应，提示GPER作为癌症治疗靶点的潜力。
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**说明**：以上文献为示例性概括，实际研究中需通过学术数据库(如PubMed、Web of Science)检索真实文献。建议使用关键词“GPER recombinant expression”、“GPER structure-function”或“GPER signaling”进一步查找。
**Background of GPER Recombinant Protein**
GPER (G protein-coupled estrogen receptor), initially identified as GPR30. is a transmembrane receptor belonging to the G protein-coupled receptor (GPCR) family. Discovered in the late 1990s, it was recognized as a novel estrogen-binding receptor distinct from classical nuclear estrogen receptors (ERα and ERβ). GPER mediates rapid, non-genomic estrogen signaling by activating intracellular pathways such as cAMP, MAPK/ERK, and PI3K/Akt, influencing processes like cell proliferation, apoptosis, and migration. Its role extends beyond reproductive tissues, impacting cardiovascular, nervous, and metabolic systems.
GPER gained attention for its involvement in hormone-related cancers (e.g., breast, ovarian) and pathologies like cardiovascular disease, making it a therapeutic target. Recombinant GPER proteins are engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional receptors for research. These proteins enable structural studies (e.g., crystallography, cryo-EM) to resolve receptor-ligand interactions and facilitate drug discovery by screening agonists/antagonists.
Recombinant GPER also aids in dissecting its signaling crosstalk with traditional estrogen receptors and androgens, clarifying its dual role in cancer progression or suppression. Challenges include optimizing recombinant protein stability and membrane localization for functional assays. Current research focuses on developing GPER-targeted therapies to mitigate side effects of conventional hormone treatments, emphasizing its potential in precision medicine.
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