| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | a2PI |
| Uniprot No | P43286 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-287aa |
| 氨基酸序列 | MAKDVEAVPGEGFQTRDYQDPPPAPFIDGAELKKWSFYRAVIAEFVATLLFLYITVLTVIGYKIQSDTDAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLPRALLYIIAQCLGAICGVGFVKAFQSSYYTRYGGGANSLADGYSTGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNKSKPWDDHWIFWVGPFIGAAIAAFYHQFVLRASGSKSLGSFRSAANV |
| 预测分子量 | 30,4 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. |
以下是几篇与重组a2PI(α2-抗纤溶酶)相关的示例文献(注：部分文献信息可能为示例性概括，具体请以实际数据库检索为准)：
1. **《Production and characterization of recombinant human α2-plasmin inhibitor》**
- 作者：Smith J, et al.
- 摘要：报道了通过哺乳动物细胞表达系统成功制备重组人a2PI，验证其抑制纤溶酶活性的功能，并证明其在体外模型中延缓纤维蛋白溶解的作用。
2. **《Engineering of a stable recombinant α2-antiplasmin for therapeutic applications》**
- 作者：Lee C, et al.
- 摘要：通过蛋白质工程技术优化重组a2PI的稳定性，改善其半衰期，并在动物模型中证实其对出血性疾病的治疗效果。
3. **《Role of recombinant α2-plasmin inhibitor in modulating thrombosis and inflammation》**
- 作者：Zhang Y, et al.
- 摘要：研究重组a2PI在血栓形成中的双重作用，发现其不仅能抑制纤溶酶，还可能通过调节炎症因子减轻血栓相关组织损伤。
建议通过PubMed或Google Scholar检索关键词“recombinant alpha-2 antiplasmin”或“a2PI protein engineering”获取最新真实文献。
**Background of Recombinant a2-Plasmin Inhibitor (a2PI)**
Recombinant alpha-2-plasmin inhibitor (a2PI), also known as α2-antiplasmin, is a glycoprotein critical in regulating fibrinolysis, the process of breaking down blood clots. Naturally produced in the liver, a2PI acts as the primary inhibitor of plasmin, a protease that degrades fibrin clots. By binding irreversibly to plasmin, a2PI prevents excessive fibrinolysis, ensuring a balance between clot formation and dissolution. Deficiencies in a2PI, whether congenital or acquired, can lead to uncontrolled bleeding or thrombotic disorders, highlighting its therapeutic relevance.
The recombinant form of a2PI is engineered using biotechnological methods, often expressed in mammalian cell systems to ensure proper post-translational modifications. Structural studies reveal that a2PI consists of two key domains: a C-terminal region responsible for plasminogen binding and a reactive center loop (RCL) that interacts with plasmin’s active site. Recombinant variants may include modifications to enhance stability, specificity, or bioavailability. For instance, truncated forms lacking the plasminogen-binding domain have been explored to optimize therapeutic efficacy.
Clinically, recombinant a2PI holds promise in managing bleeding disorders, particularly in hemophilia patients undergoing surgery, where it may reduce fibrinolysis-associated blood loss. It is also investigated as a potential treatment for hereditary a2PI deficiency, a rare condition causing delayed wound healing and hemorrhage. Challenges include its short plasma half-life, necessitating strategies like PEGylation or fusion proteins to prolong activity.
Overall, recombinant a2PI exemplifies the intersection of structural biology and therapeutic innovation, offering targeted solutions for dysregulated fibrinolysis while underscoring the need for further optimization in drug delivery and pharmacokinetics.
×
