| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | P2RX7 |
| Uniprot No | Q99572 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 47-334aa |
| 氨基酸序列 | SDKLYQRKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQGNSFFVMTNFLKTEGQEQRLCPEYPTRRTLCSSDRGCKKGWMDPQSKGIQTGRCVVHEGNQKTCEVSAWCPIEAVEEAPRPALLNSAENFTVLIKNNIDFPGHNYTTRNILPGLNITCTFHKTQNPQCPIFRLGDIFRETGDNFSDVAIQGGIMGIEIYWDCNLDRWFHHCHPKYSFRRLDDKTTNVSLYPGYNFRYAKYYKENNVEKRTLIKVFGIRFDILVFGTGGKFDIIQLV |
| 预测分子量 | 43.1 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P2RX7重组蛋白的3篇典型文献示例(内容基于研究方向概括，非真实文献)：
1. **《Recombinant human P2X7 receptor expression and functional characterization in HEK293 cells》**
- **作者**: Smith A, et al.
- **摘要**: 研究通过重组技术在HEK293细胞中表达人源P2RX7蛋白，分析了其ATP依赖性离子通道活性及细胞膜定位，证实重组蛋白在炎症信号传导中的作用。
2. **《Structural insights into the activation mechanism of the P2X7 receptor via cryo-EM》**
- **作者**: Lee B, et al.
- **摘要**: 利用冷冻电镜解析重组P2RX7蛋白的三维结构，揭示了ATP结合后受体的构象变化，为开发靶向该受体的药物提供结构基础。
3. **《Purification and functional analysis of recombinant P2X7 receptor extracellular domain》**
- **作者**: Chen Y, et al.
- **摘要**: 通过大肠杆菌系统表达并纯化P2RX7胞外结构域重组蛋白，证明其与ATP的高亲和力结合及在自身免疫疾病中的潜在应用价值。
如需真实文献，建议通过PubMed或Web of Science检索关键词“P2X7 recombinant expression/purification/function”获取近年研究。
P2RX7 (P2X purinoceptor 7) is a ligand-gated ion channel belonging to the P2X receptor family, which responds to extracellular adenosine triphosphate (ATP). Encoded by the *P2RX7* gene, it is primarily expressed in immune cells (e.g., macrophages, microglia, T-cells) and plays a critical role in inflammatory responses, apoptosis, and cellular homeostasis. Unlike other P2X receptors, P2RX7 requires high ATP concentrations for activation and uniquely forms a large transmembrane pore upon prolonged stimulation, facilitating the release of pro-inflammatory cytokines like IL-1β and IL-18. This dual functionality—ion channel and pore formation—links it to pathologies such as chronic inflammation, neurodegenerative diseases, and cancer.
Recombinant P2RX7 proteins are engineered in vitro to study its structure-function relationships, signaling mechanisms, and interactions with pharmacological modulators. These proteins are typically expressed in heterologous systems (e.g., HEK293 cells) to ensure high purity and activity. Structural studies using recombinant P2RX7 have revealed key domains involved in ATP binding, ion permeation, and pore dilation, aiding the development of selective antagonists (e.g., AZ10606120) for therapeutic targeting.
Research on recombinant P2RX7 has highlighted its dual role in health and disease. While it promotes pathogen clearance and immune surveillance, dysregulated P2RX7 activity contributes to neuroinflammation (e.g., Alzheimer’s disease), autoimmune disorders, and tumor progression. Its involvement in the NLRP3 inflammasome activation further underscores its therapeutic relevance. However, challenges remain in understanding tissue-specific regulation and reconciling discrepancies between in vitro recombinant models and in vivo physiology. Continued exploration of recombinant P2RX7 promises advancements in immunomodulatory therapies and precision medicine.
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