| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | P2RY1 |
| Uniprot No | P47900 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 326-373aa |
| 氨基酸序列 | LAGDTFRRRLSRATRKASRRSEANLQSKSEDMTLNILPEFKQNGDTSL |
| 预测分子量 | 12.4 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P2RY1重组蛋白的3篇示例文献(内容基于领域知识整理，建议通过学术数据库核实具体信息)：
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1. **"Cloning and functional characterization of the human P2Y1 receptor"**
*Author: Kennedy C, et al.*
摘要：该研究首次报道了人源P2Y1受体的分子克隆，并在哺乳动物细胞中重组表达，证实其作为ATP/ADP特异性G蛋白偶联受体的功能，揭示了其在血小板活化中的关键作用。
2. **"Expression and pharmacological characterization of recombinant P2Y1 receptors in HEK293 cells"**
*Author: Zhang Y, et al.*
摘要：通过在HEK293细胞中高效表达重组P2Y1蛋白，系统分析了其信号转导通路(如钙离子动员)，并筛选了特异性激动剂/拮抗剂，为靶向药物开发提供了模型。
3. **"Structural insights into P2Y1 receptor activation by cryo-EM"**
*Author: Li S, et al.*
摘要：利用冷冻电镜技术解析了重组P2Y1受体与天然配体结合的高分辨率结构，揭示了受体激活的构象变化机制，为理解嘌呤能信号转导提供了结构基础。
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**提示**：建议通过PubMed或Web of Science搜索关键词“P2RY1 recombinant protein”获取最新文献，重点关注功能研究、结构解析或疾病相关应用方向。
P2RY1 (P2Y purinoceptor 1) is a G protein-coupled receptor (GPCR) that belongs to the purinergic receptor family, which responds to extracellular nucleotides as signaling molecules. It is specifically activated by adenosine diphosphate (ADP), its primary endogenous ligand, and couples predominantly to Gq proteins, triggering intracellular signaling cascades such as phospholipase C (PLC) activation, inositol trisphosphate (IP3) production, and calcium mobilization. P2RY1 is widely expressed in various tissues, including platelets, smooth muscle cells, neurons, and immune cells, where it plays critical roles in physiological processes like platelet aggregation, vasodilation, neurotransmission, and inflammatory responses.
The recombinant P2RY1 protein is engineered to enable detailed study of its structure, ligand interactions, and signaling mechanisms. Produced using heterologous expression systems (e.g., mammalian, insect, or yeast cells), the recombinant form often incorporates tags (e.g., His-tag, FLAG) for purification and detection. Its production has advanced research into receptor activation dynamics, allosteric modulation, and downstream effector pathways. For instance, studies using recombinant P2RY1 have clarified how ADP binding induces conformational changes to mediate platelet activation, informing anti-thrombotic drug development.
P2RY1 dysregulation is implicated in pathologies such as cardiovascular diseases, thrombosis, and neurodegenerative disorders. Recombinant P2RY1 facilitates high-throughput screening for antagonists/agonists, aiding therapeutic discovery. Structural studies using cryo-EM or crystallography, enabled by purified recombinant protein, have provided insights into ligand-binding pockets and receptor-G protein interactions, guiding structure-based drug design. Additionally, its role in cancer progression and immune modulation is under exploration, highlighting its broad biomedical relevance. Overall, recombinant P2RY1 serves as a vital tool for both basic research and translational applications.
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