| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Serpine1 |
| Uniprot No | P05121 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-402aa |
| 氨基酸序列 | VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTT GGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQ RDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISN LLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVP MMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSAL TNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR QFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPE EIIMDRPFLFVVRHNPTGTVLFMGQVMEP |
| 预测分子量 | 43 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Serpine1(PAI-1)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*High-level synthesis of functional human plasminogen activator inhibitor type 1 (PAI-1) in Escherichia coli*
**作者**：Ny, T., Sawdey, M., Lawrence, D., et al.
**摘要**：该研究报道了在大肠杆菌中高效表达重组人PAI-1的方法，并通过亲和层析纯化获得高活性蛋白。实验证明重组PAI-1能有效抑制组织型纤溶酶原激活剂(t-PA)，为后续功能研究提供了可靠来源。
2. **文献名称**：*Crystal structure of the catalytic domain of human plasminogen activator inhibitor-1*
**作者**：Zhou, A., Huntington, J.A., Pannu, N.S., et al.
**摘要**：通过X射线晶体学解析了PAI-1催化结构域的三维结构，揭示了其与靶标蛋白酶(如尿激酶型纤溶酶原激活剂)结合的分子机制，为设计特异性抑制剂奠定结构基础。
3. **文献名称**：*PAI-1 inhibits urokinase-induced vitronectin adhesion by competing for binding to the urokinase receptor*
**作者**：Gorlatova, N.V., Czekay, R.P., Lawrence, D.A., et al.
**摘要**：研究发现重组PAI-1通过竞争性结合尿激酶受体(uPAR)抑制细胞黏附，并证实PAI-1与玻连蛋白(vitronectin)的相互作用可延长其半衰期，提示其在细胞迁移和肿瘤微环境中的调控作用。
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这些研究涵盖了重组PAI-1的生产、结构解析及功能机制，适用于疾病模型构建或药物开发参考。如需具体文献，建议通过PubMed或Sci-Hub输入标题或DOI进一步获取全文。
Serpine1. also known as plasminogen activator inhibitor-1 (PAI-1), is a member of the serine protease inhibitor (serpin) superfamily. It functions as a key regulator of the fibrinolytic system by inhibiting tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), enzymes responsible for converting plasminogen to plasmin, a protease that degrades fibrin clots. By controlling fibrinolysis, Serpine1 plays a critical role in maintaining hemostatic balance, tissue remodeling, and cell migration.
Physiologically, PAI-1 is involved in wound healing, angiogenesis, and extracellular matrix dynamics. However, its dysregulation is linked to pathological conditions. Elevated PAI-1 levels are associated with thrombotic disorders due to impaired clot dissolution, as well as fibrotic diseases, metabolic syndrome, and cancer progression. In cancer, PAI-1 exhibits paradoxical roles: it inhibits proteolytic activity to limit metastasis but also promotes tumor cell survival, angiogenesis, and stromal interactions through non-proteolytic mechanisms.
Recombinant Serpine1 protein is produced using genetic engineering techniques, often expressed in Escherichia coli, yeast, or mammalian cell systems to ensure proper folding and post-translational modifications. This recombinant form retains the functional domains of native PAI-1. including the reactive center loop (RCL) that interacts with target proteases and binding sites for vitronectin, a glycoprotein that stabilizes PAI-1 activity. Researchers utilize recombinant Serpine1 to study its structure-function relationships, signaling pathways, and interactions with other molecules in vitro and in vivo.
Its therapeutic relevance spans anticoagulant drug development, antifibrotic strategies, and cancer therapy. Inhibitors targeting PAI-1 are under investigation to counteract its pathological effects, while recombinant PAI-1 itself has been explored as a potential therapeutic agent in bleeding disorders. The protein’s dual role in health and disease underscores its importance as a research target and biomarker in translational medicine.
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