| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OPRM1 |
| Uniprot No | P35372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-400aa |
| 氨基酸序列 | MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRT DLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTK MKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDY YNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAI GLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLII TVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHI YVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFR EFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP |
| 预测分子量 | 45 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OPRM1(μ-阿片受体)重组蛋白的3篇代表性文献概览：
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1. **文献名称**: *Crystal structure of the μ-opioid receptor bound to a morphinan antagonist*
**作者**: Manglik, A. et al.
**摘要**: 该研究通过重组表达技术在大肠杆菌中制备了人源OPRM1蛋白，并利用X射线晶体学解析了其与拮抗剂β-氯纳曲酮结合的复合物结构。首次揭示了μ受体跨膜区的三维构象，为理解阿片类药物的作用机制提供了结构基础。
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2. **文献名称**: *Structure of the μ-opioid receptor–Gi protein complex*
**作者**: Koehl, A. et al.
**摘要**: 利用昆虫细胞表达系统重组OPRM1蛋白，结合冷冻电镜技术解析了受体与Gi蛋白复合物的高分辨率结构。研究阐明了μ受体激活后与下游信号蛋白偶联的分子机制，为开发副作用更小的镇痛药物提供了新思路。
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3. **文献名称**: *Recombinant expression and functional characterization of human μ-opioid receptor in Saccharomyces cerevisiae*
**作者**: Zhang, Y. et al.
**摘要**: 成功在酵母系统中重组表达功能性OPRM1蛋白，并验证其与阿片类配体(如吗啡和纳洛酮)的特异性结合能力。该表达系统为高通量筛选受体激动剂/拮抗剂提供了低成本平台。
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4. **文献名称**: *Biosynthesis and characterization of a fluorescently labeled μ-opioid receptor for single-molecule imaging*
**作者**: Stoeber, M. et al.
**摘要**: 在哺乳动物细胞中重组表达带有荧光标记的OPRM1蛋白，结合单分子显微镜技术实时观察受体在细胞膜上的动态分布及内化过程，揭示了阿片类药物诱导受体脱敏的时空调控机制。
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这些研究覆盖了OPRM1重组蛋白的结构解析、信号机制、表达系统开发及动态功能分析等方向。如需具体文献链接或补充年份信息，可进一步说明。
The μ-opioid receptor (MOR), encoded by the **OPRM1 gene**, is a G protein-coupled receptor (GPCR) central to pain modulation, reward pathways, and addiction. It serves as the primary target for endogenous opioids (e.g., endorphins) and exogenous opiates (e.g., morphine, fentanyl). Dysregulation of MOR signaling is implicated in chronic pain, opioid tolerance, and substance use disorders. Recombinant OPRM1 protein refers to the engineered form of this receptor, typically expressed in heterologous systems (e.g., HEK293 or CHO cells) for structural, functional, and pharmacological studies.
Recombinant OPRM1 allows researchers to study receptor-ligand interactions, signal transduction mechanisms (e.g., G protein vs. β-arrestin pathways), and the effects of genetic polymorphisms (e.g., the A118G SNP linked to altered drug responses). Its production often involves tagging (e.g., FLAG, His-tag) for purification and visualization. Structural studies using recombinant MOR, such as X-ray crystallography and cryo-EM, have revealed binding pockets for opioids and allosteric modulators, guiding the design of safer analgesics.
Despite advances, challenges remain, including preserving native receptor conformation in vitro and replicating complex in vivo interactions (e.g., with membrane lipids or accessory proteins). Recombinant OPRM1 remains indispensable for high-throughput drug screening and mechanistic studies aimed at addressing the opioid crisis and improving pain therapies.
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