| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPSR |
| Uniprot No | Q6W5P4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-371aa |
| 氨基酸序列 | MPANFTEGSFDSSGTGQTLDSSPVACTETVTFTEVVEGKEWGSFYYSFKTEQLITLWVLFVFTIVGNSVVLFSTWRRKKKSRMTFFVTQLAITDSFTGLVNILTDINWRFTGDFTAPDLVCRVVRYLQVVLLYASTYVLVSLSIDRYHAIVYPMKFLQGEKQARVLIVIAWSLSFLFSIPTLIIFGKRTLSNGEVQCWALWPDDSYWTPYMTIVAFLVYFIPLTIISIMYGIVIRTIWIKSKTYETVISNCSDGKLCSSYNRGLISKAKIKAIKYSIIIILAFICCWSPYFLFDILDNFNLLPDTQERFYASVIIQNLPALNSAINPLIYCVFSSSISFPCREQRSQDSRMTFRERTERHEMQILSKPEFI |
| 预测分子量 | 42,6 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NPSR(神经肽S受体)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Expression, Purification, and Structural Analysis of the Human Neuropeptide S Receptor*
**作者**：Smith, J. et al.
**摘要**：本研究在大肠杆菌中表达了重组人源NPSR蛋白，通过亲和层析和尺寸排阻色谱纯化，获得高纯度蛋白。利用冷冻电镜技术解析了NPSR与其天然配体神经肽S的结合结构，揭示了受体激活的关键构象变化，为靶向药物设计提供了结构基础。
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2. **文献名称**：*Functional Characterization of Recombinant NPSR in a Cellular Model of Airway Inflammation*
**作者**：Jones, L. & Wang, H.
**摘要**：作者在HEK293细胞中过表达重组NPSR，发现其激活后显著增强IL-8分泌并促进NF-κB信号通路。研究证实NPSR在呼吸道炎症中的潜在作用，为哮喘等疾病的治疗靶点提供了实验依据。
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3. **文献名称**：*Development of a Bioluminescence Resonance Energy Transfer (BRET) Assay for NPSR Ligand Screening*
**作者**：Brown, K. et al.
**摘要**：通过构建重组NPSR与G蛋白偶联的BRET报告系统，建立了一种高通量筛选方法，成功鉴定出多个新型NPSR拮抗剂。该平台为神经精神疾病和炎症相关药物的开发提供了高效工具。
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**备注**：上述文献为模拟示例，实际研究中建议通过PubMed或Web of Science以关键词“Neuropeptide S Receptor recombinant”检索最新文献。
Neuropeptide S receptor (NPSR), a class A G protein-coupled receptor (GPCR), plays a critical role in modulating physiological processes such as anxiety, arousal, feeding, and inflammatory responses. Discovered in the early 2000s, NPSR binds its endogenous ligand, neuropeptide S (NPS), to activate intracellular signaling pathways, primarily via Gαs-mediated cAMP production. It is expressed in the central nervous system and peripheral tissues, including immune cells, linking neuroendocrine and immune functions. Dysregulation of NPSR signaling has been implicated in disorders like anxiety, asthma, and inflammatory bowel disease, making it a therapeutic target.
Recombinant NPSR proteins are engineered for structural and functional studies. Produced using heterologous expression systems (e.g., HEK293 or Sf9 cells), these proteins retain key receptor features, such as ligand-binding specificity and post-translational modifications. To enhance stability and solubility, researchers often fuse NPSR with tags like His or FLAG for purification and detection. Structural studies using recombinant NPSR have revealed ligand-binding pockets and activation mechanisms, aiding drug design. For example, X-ray crystallography and cryo-EM analyses of NPSR-ligand complexes provide insights into conformational changes during receptor activation.
Applications of recombinant NPSR include high-throughput drug screening, receptor-ligand interaction assays, and mechanistic studies of signaling pathways. It also aids in developing antibodies or biosensors to monitor receptor dynamics in vitro or in vivo. Recent advances focus on biased agonists that selectively activate therapeutic pathways while minimizing side effects. Despite challenges like receptor instability and low yield, optimized expression protocols continue to advance NPSR-related research, bridging gaps between molecular understanding and clinical applications.
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