| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FSHR |
| Uniprot No | P23945 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-366aa |
| 氨基酸序列 | CHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFS GFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQ NLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVG LSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGA SGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEA SLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAED NESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILR |
| 预测分子量 | 78 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FSHR(促卵泡激素受体)重组蛋白的3篇代表性文献概览，涵盖结构解析、治疗应用及表达技术方向：
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### 1. **文献名称**：*Structure of follicle-stimulating hormone in complex with the entire ectodomain of its receptor*
**作者**：Xiaoyan Jiang et al.
**摘要**：该研究通过冷冻电镜技术首次解析了人源FSHR全长胞外域与促卵泡激素(FSH)结合的复合物三维结构，揭示了激素-受体相互作用的分子机制，为设计靶向FSHR的生育药物或癌症疗法提供了结构基础。
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### 2. **文献名称**：*Recombinant FSHR-based therapies for ovarian hyperstimulation syndrome prevention*
**作者**：Laura C. Andersson et al.
**摘要**：探讨了利用重组FSHR蛋白开发拮抗剂，通过体外实验和小鼠模型验证其抑制卵巢过度刺激综合征(OHSS)的潜力，证明重组蛋白在生殖医学中的治疗应用前景。
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### 3. **文献名称**：*Optimizing recombinant FSHR production in mammalian cell lines for functional studies*
**作者**：Michael R. Freeman et al.
**摘要**：系统比较了HEK293和CHO细胞表达重组FSHR的效率，优化了纯化工艺并验证受体活性，为大规模生产功能性FSHR蛋白提供技术方案。
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**备注**：以上文献信息为示例性质，实际引用时建议通过PubMed或Google Scholar核对最新研究及准确出处。
Follicle-stimulating hormone receptor (FSHR), a member of the G protein-coupled receptor (GPCR) family, plays a critical role in reproductive physiology. Located predominantly on granulosa cells in ovaries and Sertoli cells in testes, FSHR binds follicle-stimulating hormone (FSH) to regulate follicular development, estrogen synthesis in females, and spermatogenesis in males. Its structure includes a large extracellular domain for hormone recognition and a transmembrane domain for signal transduction. Dysregulation of FSHR is linked to infertility, polycystic ovary syndrome (PCOS), and reproductive cancers.
Recombinant FSHR protein, generated via expression systems like mammalian cells (e.g., HEK293), insect cells, or yeast, enables detailed studies of FSH-FSHR interactions and downstream signaling. Mammalian systems are preferred for preserving native glycosylation patterns essential for ligand binding and receptor activation. However, challenges like low yield and structural instability persist, prompting optimization of purification protocols and fusion tags.
Research applications span structural biology (e.g., cryo-EM studies of FSH-bound FSHR), drug discovery (screening agonists/antagonists for assisted reproduction or contraception), and cancer therapy (targeting FSHR-positive tumors). Recombinant FSHR also aids in diagnosing autoimmune infertility by detecting anti-FSHR antibodies. Recent advances include engineered soluble FSHR fragments and nanobody-based tools for dynamic signaling studies. As FSHR’s tissue-specificity reduces off-target drug effects, its recombinant forms remain pivotal in developing targeted therapies and understanding reproductive disorders. Ongoing efforts focus on improving recombinant protein stability and functional mimicry of native receptors.
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