纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OPRD1 |
Uniprot No | P41143 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-372aa |
氨基酸序列 | MEPAPSAGAELQPPLFANASDAYPSACPSAGANASGPPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTACTPSDGPGGGAAA |
预测分子量 | 41.9 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OPRD1重组蛋白的3篇参考文献,简要概括核心内容:
1. **《Expression and Purification of Recombinant Human δ-Opioid Receptor in Insect Cells》**
*作者:Smith A, et al.*
摘要:研究利用杆状病毒-昆虫细胞表达系统高效表达人源OPRD1重组蛋白,优化纯化流程获得高纯度受体,用于体外配体结合实验及功能分析。
2. **《Structural Insights into δ-Opioid Receptor Activation Using a Nanobody-Stabilized Active State》**
*作者:Zhang Y, et al.*
摘要:通过纳米抗体稳定OPRD1的活性构象,结合冷冻电镜技术解析其三维结构,揭示了受体与G蛋白偶联的分子机制及潜在药物靶点。
3. **《Functional Characterization of Recombinant δ-Opioid Receptor Mutants in Pain Modulation》**
*作者:Lee J, et al.*
摘要:在大肠杆菌中表达OPRD1突变体重组蛋白,研究关键位点突变对受体信号传导的影响,发现特定区域在疼痛调节中的功能差异。
(注:以上文献为示例,实际文献需通过PubMed或专业数据库查询确认。)
The delta-opioid receptor (δ-OR, encoded by the *OPRD1* gene) is a G protein-coupled receptor (GPCR) predominantly expressed in the central and peripheral nervous systems. It plays a critical role in modulating pain perception, emotional responses, and neuropsychiatric functions by binding endogenous opioid peptides (e.g., enkephalins) and synthetic ligands. Unlike mu-opioid receptors (associated with analgesia and addiction), δ-OR activation is linked to anxiolytic, antidepressant, and less addictive properties, making it a promising therapeutic target for chronic pain, mood disorders, and addiction.
Recombinant OPRD1 proteins are engineered in vitro using heterologous expression systems (e.g., mammalian cells, *E. coli*, or yeast) to study receptor structure, signaling, and ligand interactions. These proteins often include tags (e.g., His-tag, FLAG) for purification and detection. Researchers utilize OPRD1 recombinant proteins to elucidate ligand-binding mechanisms, receptor dimerization, and downstream signaling pathways (e.g., Gi/o protein coupling, MAPK/ERK activation). Structural studies (X-ray crystallography, cryo-EM) of recombinant δ-OR have revealed key conformational changes during activation, aiding rational drug design.
Despite challenges like low native expression and instability, recombinant OPRD1 enables high-throughput screening of selective agonists/antagonists and probes receptor dysfunction in neurological diseases. Its study bridges gaps in opioid receptor pharmacology, offering insights into safer analgesics and neuropsychiatric therapies.
×