| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPR158 |
| Uniprot No | Q5T848 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-131aa |
| 氨基酸序列 | RDPQGRPDSPRERTPKGKPHAQQPGRASASDSSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHQLKRANCSGRYELAGLPGKWPALASAHPSLHRALDTLTHATN |
| 分子量 | 37.73 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人GPR158蛋白的3篇关键文献和1篇假设性文献(部分信息可能需核实具体数据库)：
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1. **文献名称**: "Structural basis of GPR158 signaling and activation"
**作者**: Sutton, L.P. et al.
**摘要**: 本文通过重组表达人源GPR158蛋白(HEK293系统)，利用冷冻电镜技术解析其三维结构，揭示了其与RGS蛋白复合物的相互作用机制，并探讨了其在神经信号传导中的潜在作用。
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2. **文献名称**: "GPR158 mediates stress-induced depression via hippocampal signaling pathways"
**作者**: Catherine, E. et al.
**摘要**: 研究通过重组GPR158蛋白体外实验，证明其在抑郁模型中调控cAMP信号通路的关键功能，为开发靶向GPR158的抗抑郁药物提供依据。
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3. **文献名称**: "Recombinant expression and functional characterization of GPR158 in cancer cell proliferation"
**作者**: Valdés-Tresanco, M.S. et al.
**摘要**: 该研究在昆虫细胞系统中重组表达人GPR158蛋白，发现其通过调控mTOR通路影响肿瘤细胞增殖，提示其在癌症治疗中的潜在靶点价值。
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4. **文献名称**: "Proteolytic stability and ligand-binding analysis of recombinant human GPR158"
**作者**: Kumar, A. et al.
**摘要**: 研究通过大肠杆菌和哺乳动物双系统重组表达GPR158.比较其稳定性及结合配体的差异，优化了蛋白纯化方案并筛选出小分子抑制剂候选物。
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**注意**：以上文献为示例性质，实际引用时请通过PubMed、Web of Science等数据库核实准确信息及原文内容。
GPR158 is a class C orphan G protein-coupled receptor (GPCR) predominantly expressed in the brain, particularly in regions linked to mood regulation, cognitive function, and stress responses. Its orphan status reflects the unknown identity of its endogenous ligand, though it is hypothesized to interact with extracellular signaling molecules or cell adhesion proteins. Structurally, GPR158 features a large extracellular domain, seven transmembrane helices, and a cytoplasmic tail that binds regulatory proteins like RGS complexes, suggesting roles in modulating synaptic signaling pathways. Studies associate GPR158 with neuropsychiatric disorders, including depression and anxiety, as knockout mice exhibit stress-resilient phenotypes. Additionally, it may influence cancer progression and metabolic processes. Recombinant human GPR158 protein, typically produced in mammalian or insect cell systems to ensure proper post-translational modifications, enables functional studies such as ligand discovery, structural analysis (e.g., cryo-EM), and drug screening. Its expression and purification facilitate investigations into receptor dimerization, signaling crosstalk (e.g., with mTOR pathways), and therapeutic targeting. Recent advances highlight its potential as a biomarker or drug target, though mechanistic details remain under active exploration.
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