| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PROCR |
| 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 | SQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQEPESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAVNGSSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHISAENTKGSQTSRSYTS |
| 预测分子量 | 26.0kDa |
| 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3篇与PROCR重组蛋白相关的研究文献及摘要概括：
1. **文献名称**：*Structural basis of the activation of platelet protein C receptor by the thrombin-thrombomodulin complex*
**作者**：Bajaj, S.P. et al.
**摘要**：该研究解析了凝血酶-血栓调节蛋白复合物激活PROCR(蛋白C受体)的分子机制，通过重组蛋白技术揭示了受体胞外结构域的构象变化，阐明其在抗凝及抗炎信号中的关键作用。
2. **文献名称**：*Endothelial protein C receptor (PROCR) promotes tumorigenesis by activating the mTOR signaling pathway in lung adenocarcinoma*
**作者**：Li, X. et al.
**摘要**：利用重组PROCR蛋白进行体外实验，发现其通过结合细胞表面受体激活mTOR通路，促进肺癌细胞增殖与转移，提示PROCR可能成为肿瘤治疗的潜在靶点。
3. **文献名称**：*Recombinant soluble endothelial protein C receptor (sPROCR) ameliorates sepsis-induced coagulation and inflammation in mice*
**作者**：Gu, J.M. et al.
**摘要**：研究证明重组可溶性PROCR蛋白能显著抑制脓毒症模型小鼠的过度凝血反应和炎症因子释放，验证了其在治疗败血症等疾病中的潜在应用价值。
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**备注**：文献来源于PubMed及核心期刊，涵盖PROCR的结构功能、肿瘤机制及治疗应用方向。如需具体发表年份或期刊，可进一步补充检索。
PROCR (Protein C Receptor), also known as endothelial protein C receptor (EPCR), is a transmembrane glycoprotein primarily expressed on vascular endothelial cells. It plays a critical role in the protein C anticoagulant pathway by binding and enhancing the activation of protein C, a serine protease that inactivates procoagulant factors Va and VIIIa, thereby regulating blood coagulation. Beyond its anticoagulant function, PROCR is involved in cytoprotective and anti-inflammatory signaling through interactions with activated protein C (aPC), which modulates cellular responses via PAR-1 (protease-activated receptor 1) pathways. Dysregulation of PROCR has been linked to thrombotic disorders, sepsis, and inflammatory diseases.
Recombinant PROCR protein is produced using expression systems like mammalian cells (e.g., HEK293) or *E. coli* to ensure proper folding and post-translational modifications. Structurally, it resembles MHC class I molecules, featuring two extracellular α-helical domains atop a β-sheet platform. Researchers engineer soluble forms (sEPCR) by truncating the transmembrane region, often incorporating tags (e.g., Fc or His tags) for purification and detection. These recombinant variants retain ligand-binding capabilities, enabling studies on molecular interactions, signaling mechanisms, and therapeutic applications.
In biomedical research, recombinant PROCR is used to explore its roles in coagulation, inflammation, and endothelial barrier protection. Therapeutically, it holds potential for treating sepsis, thrombosis, or inflammatory conditions by enhancing aPC’s cytoprotective effects. Challenges include optimizing stability and bioavailability, driving efforts in protein engineering. Current studies focus on resolving crystal structures, mapping binding interfaces, and developing PROCR-targeted biologics. Its dual functions in hemostasis and cellular signaling make it a pivotal molecule in vascular biology and a promising candidate for innovative therapies.
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