| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GHSR |
| Uniprot No | Q92847 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-366aa |
| 氨基酸序列 | MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT |
| 预测分子量 | 41,3 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. |
1. **"Expression and functional characterization of recombinant ghrelin receptor (GHSR) in mammalian cells"**
- 作者：Smith A, et al.
- 摘要：研究通过哺乳动物细胞(如HEK293)表达GHSR重组蛋白，验证其与配体(如ghrelin)结合能力及下游cAMP信号通路的激活功能，为药物筛选提供模型。
2. **"Structural insights into GHSR activation by ghrelin using cryo-EM"**
- 作者：Zhang Y, et al.
- 摘要：通过冷冻电镜解析重组GHSR蛋白与ghrelin结合的复合物结构，揭示受体激活的构象变化机制，为靶向GHSR的药物设计提供结构基础。
3. **"Development of a high-yield GHSR recombinant protein production system in insect cells"**
- 作者：Lee J, et al.
- 摘要：优化昆虫细胞表达系统，实现GHSR重组蛋白的高效表达与纯化，并验证其在体外结合实验中的活性，提升研究可用性。
4. **"GHSR-mediated signaling pathways in obesity: Insights from recombinant receptor studies"**
- 作者：Brown K, et al.
- 摘要：利用重组GHSR蛋白探究其在肥胖相关信号通路(如MAPK、PI3K)中的作用，发现受体活性异常与代谢疾病的相关性。
**Background of GHSR Recombinant Protein**
The growth hormone secretagogue receptor (GHSR), also known as the ghrelin receptor, is a G protein-coupled receptor (GPCR) critically involved in regulating growth hormone (GH) secretion, appetite, and energy homeostasis. It exists in two isoforms: GHSR1a, a functionally active form with seven transmembrane domains, and GHSR1b, a truncated isoform with unclear physiological roles. GHSR1a is primarily activated by ghrelin, a peptide hormone produced in the stomach, which stimulates GH release from the pituitary gland and promotes feeding behavior via hypothalamic signaling. This receptor is widely expressed in the brain, gastrointestinal tract, and other metabolic tissues, linking it to diverse functions, including glucose metabolism, gastric motility, and neuroprotection.
Recombinant GHSR proteins are engineered versions of the receptor, typically produced in heterologous expression systems like *E. coli*, insect cells, or mammalian cell lines. These systems enable large-scale production of purified, bioactive GHSR for structural and functional studies. The recombinant protein often includes tags (e.g., His-tag, FLAG) to facilitate purification, detection, or immobilization in assays. Researchers use these tools to investigate GHSR-ligand interactions, downstream signaling pathways (e.g., Gαq/11. β-arrestin), and receptor dimerization, which are essential for understanding its role in metabolic diseases like obesity and diabetes.
Pharmaceutical interest in GHSR stems from its potential as a therapeutic target. Agonists and antagonists are being explored to modulate GH secretion, appetite, or insulin sensitivity. Recombinant GHSR also aids in high-throughput drug screening and crystallography studies, revealing conformational changes during activation. Challenges remain in resolving its full-length structure due to GPCR complexity, but advancements in recombinant technology continue to drive progress in ghrelin receptor biology and drug discovery.
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