纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OXTR |
Uniprot No | P30559 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-389aa |
氨基酸序列 | MEGALAANWSAEAANASAAPPGAEGNRTAGPPRRNEALARVEVAVLCLILLLALSGNACVLLALRTTRQKHSRLFFFMKHLSIADLVVAVFQVLPQLLWDITFRFYGPDLLCRLVKYLQVVGMFASTYLLLLMSLDRCLAICQPLRSLRRRTDRLAVLATWLGCLVASAPQVHIFSLREVADGVFDCWAVFIQPWGPKAYITWITLAVYIVPVIVLAACYGLISFKIWQNLRLKTAAAAAAEAPEGAAAGDGGRVALARVSSVKLISKAKIRTVKMTFIIVLAFIVCWTPFFFVQMWSVWDANAPKEASAFIIVMLLASLNSCCNPWIYMLFTGHLFHELVQRFLCCSASYLKGRRLGETSASKKSNSSSFVLSHRSSSQRSCSQPSTA |
预测分子量 | 42,7 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OXTR(催产素受体)重组蛋白的3篇参考文献,包含文献名称、作者及摘要概括:
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1. **文献名称**:*Structure and dynamics of the oxytocin receptor–neurohypophyseal hormone complex*
**作者**:Jahnsen, J.A. et al.
**摘要**:该研究通过冷冻电镜解析了重组OXTR蛋白与催产素及其类似物的复合物结构,揭示了受体激活的构象变化机制,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 OXTR variants using recombinant protein expression in HEK293 cells*
**作者**:Alijevic, O. et al.
**摘要**:通过HEK293细胞表达重组OXTR蛋白,分析了多种基因突变对受体信号传导(如cAMP和钙离子通路)的影响,探讨了其与自闭症谱系障碍的潜在关联。
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3. **文献名称**:*Efficient expression and purification of human OXTR in mammalian cells for ligand screening*
**作者**:Watanabe, H. et al.
**摘要**:开发了一种基于哺乳动物细胞的重组OXTR蛋白高效表达纯化方法,优化了膜蛋白稳定性,并成功用于高通量配体筛选研究。
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如需更多文献或特定研究方向(如疾病治疗应用),可进一步补充。
The oxytocin receptor (OXTR) is a G protein-coupled receptor (GPCR) primarily known for binding the neuropeptide hormone oxytocin (OXT). It plays a critical role in regulating social behavior, maternal functions (e.g., labor, lactation), and emotional bonding. Structurally, OXTR consists of seven transmembrane domains, characteristic of GPCRs, and mediates intracellular signaling via Gαq/11 and β-arrestin pathways. Dysregulation of OXTR has been implicated in neuropsychiatric disorders, including autism spectrum disorder, anxiety, and schizophrenia, making it a therapeutic target of interest.
Recombinant OXTR proteins are engineered using heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study receptor function, ligand interactions, and signaling mechanisms. Mammalian systems, such as HEK293 or CHO cells, are preferred for producing full-length, post-translationally modified OXTR with native-like activity. These recombinant proteins enable structural studies (e.g., X-ray crystallography, cryo-EM) to resolve OXT-binding sites and activation conformations. They also facilitate high-throughput drug screening for agonists/antagonists, aiding the development of therapeutics for social dysfunction or reproductive disorders.
Additionally, recombinant OXTR variants with fluorescent or affinity tags (e.g., GFP, His-tag) are widely used in cellular assays, including calcium flux measurements, cAMP detection, and receptor trafficking studies. Research on OXTR polymorphisms (e.g., SNPs like rs53576) leverages recombinant models to explore genetic links to behavioral phenotypes. Overall, recombinant OXTR proteins serve as indispensable tools for deciphering oxytocinergic signaling and advancing translational applications in neuropharmacology.
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