| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPCR |
| Uniprot No | Q9UNN8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-210aa |
| 氨基酸序列 | SQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTI IQLQPLQEPESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLG CELPPEGSRAHVFFEVAVNGSSFVSFRPERALWQADTQVTSGVVTFTLQQ LNAYNRTRYELREFLEDTCVQYVQKHISAENTKGSQTSRSYTSVDHHHHH H |
| 预测分子量 | 23 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EPCR重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: **"Cloning and characterization of the endothelial protein C receptor (EPCR) gene"**
**作者**: Fukudome K, Esmon CT
**摘要**: 该研究首次成功克隆并表达了人源EPCR的重组蛋白，利用哺乳动物细胞系统进行表达，证实其与活性蛋白C(APC)的高亲和力结合，并揭示了EPCR在内皮细胞抗凝血功能中的关键作用。
2. **文献名称**: **"Recombinant endothelial protein C receptor improves survival in murine sepsis through anti-inflammatory and anticoagulant mechanisms"**
**作者**: Kerschen EJ, et al.
**摘要**: 通过动物模型研究发现，外源性重组EPCR蛋白显著降低败血症小鼠的死亡率，其机制涉及抑制过度炎症反应和调节凝血级联，为EPCR的潜在治疗应用提供了实验依据。
3. **文献名称**: **"Crystal structure of the endothelial protein C receptor (EPCR) in complex with a lipid-binding site"**
**作者**: Oganesyan V, et al.
**摘要**: 本研究解析了重组EPCR蛋白的晶体结构，揭示了其磷脂结合域的三维构象及与配体相互作用的分子机制，为设计靶向EPCR的药物奠定了基础。
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这些文献涵盖了EPCR重组蛋白的早期发现、功能验证及结构解析，体现了其在基础研究与治疗开发中的重要性。如需更多领域相关研究，可进一步扩展至肿瘤或信号通路方向。
Endothelial Protein C Receptor (EPCR), encoded by the *PROCR* gene, is a transmembrane glycoprotein belonging to the CD1/major histocompatibility complex family. Initially identified on vascular endothelial cells, EPCR binds protein C and activated protein C (APC) with high affinity, playing a pivotal role in regulating coagulation, inflammation, and cellular signaling. By enhancing APC generation, EPCR promotes anticoagulant activity through the inactivation of coagulation factors Va and VIIIa. Beyond hemostasis, EPCR-APC signaling activates protease-activated receptor 1 (PAR1), triggering cytoprotective pathways that mitigate inflammation, apoptosis, and endothelial barrier disruption.
Recombinant EPCR proteins, typically produced in mammalian systems (e.g., CHO or HEK293 cells), are engineered to mimic native EPCR’s structure and function. These proteins often include soluble variants (sEPCR) lacking the transmembrane domain, fused with tags (e.g., Fc or His tags) for purification and detection. Structural studies reveal EPCR’s hydrophobic groove as the binding site for APC’s Gla domain, a feature critical for its anticoagulant activity.
Research applications of recombinant EPCR span mechanistic studies of sepsis, thrombosis, and inflammatory diseases, as well as therapeutic exploration for conditions like ischemic stroke and cancer. Dysregulated EPCR expression is linked to pathologies such as atherosclerosis and metastatic cancer, highlighting its dual roles in homeostasis and disease. Additionally, recombinant EPCR serves as a tool to investigate interactions with pathogens (e.g., malaria parasites) that exploit EPCR for host cell invasion. Despite therapeutic promise, challenges include balancing its anticoagulant benefits against potential risks of bleeding and understanding context-dependent signaling outcomes. Ongoing studies aim to harness EPCR’s multifaceted biology for targeted therapies and biomarker development.
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