| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TFPI |
| Uniprot No | P10646-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 152-251aa |
| 氨基酸序列 | RFKYGGCLGNMNNFETLEECKNICEDGPNGFQVDNYGTQLNAVNNSLTPQ STKVPSLFVTKEGTNDGWKSAAHIYQVFLNAFCIHASMFFLGLDSISCLC |
| 预测分子量 | 37 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3-4条关于TFPI(组织因子途径抑制物)重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*Recombinant tissue factor pathway inhibitor prevents thrombosis without increased bleeding in rabbits*
**作者**：B. P. Wood et al.
**摘要**：该研究通过动物模型(兔)验证了重组TFPI的抗凝效果，表明其能有效抑制血栓形成，且未增加出血风险，提示其作为抗凝治疗的潜在安全性。
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2. **文献名称**：*TFPI inhibits endotoxin-induced coagulation and inflammation in a primate sepsis model*
**作者**：E. Abraham et al.
**摘要**：研究在灵长类脓毒症模型中评估重组TFPI的作用，发现其通过抑制组织因子介导的凝血和炎症反应，显著改善存活率，支持其在脓毒症治疗中的应用潜力。
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3. **文献名称**：*Pharmacokinetics of recombinant TFPI in healthy volunteers*
**作者**：J. B. Hansen et al.
**摘要**：该临床试验分析了健康受试者中重组TFPI的药代动力学特性，结果显示其半衰期较短但耐受性良好，为后续剂量优化提供了依据。
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4. **文献名称**：*Structure-function analysis of TFPI using recombinant protein variants*
**作者**：T. J. Girard et al.
**摘要**：通过构建重组TFPI突变体，研究揭示了其Kunitz结构域与凝血因子Xa和VIIa的相互作用机制，为设计改良型抗凝药物奠定理论基础。
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以上文献涵盖动物实验、临床研究及分子机制分析，均聚焦于重组TFPI的抗凝、抗炎作用及潜在治疗价值。
Tissue Factor Pathway Inhibitor (TFPI) is a natural anticoagulant protein that regulates the extrinsic coagulation pathway, primarily produced by endothelial cells and megakaryocytes. It inhibits thrombin generation by neutralizing the factor VIIa/tissue factor (FVIIa/TF) complex and factor Xa (FXa), thereby preventing excessive blood clotting. Native TFPI contains three Kunitz-type domains: the first binds FVIIa/TF, the second inhibits FXa, and the third’s role remains less defined. Its anticoagulant activity is enhanced through interactions with protein S and heparan sulfate proteoglycans.
Recombinant TFPI (rTFPI) is a bioengineered version developed to overcome limitations of plasma-derived TFPI, such as low natural abundance and purification challenges. Produced using mammalian cell cultures or bacterial systems, rTFPI retains the functional domains of endogenous TFPI while offering scalable production and consistent quality. Research has focused on its therapeutic potential in coagulopathies, including sepsis-associated disseminated intravascular coagulation (DIC) and hemophilia, where unbalanced coagulation contributes to pathology. Early clinical trials suggested benefits in reducing mortality in severe sepsis, though later studies showed mixed outcomes, highlighting dose-dependent effects and context-specific activity.
Ongoing studies explore engineered variants, such as TFPIα derivatives or PEGylated forms, to improve pharmacokinetics and tissue targeting. rTFPI also serves as a tool to investigate crosstalk between coagulation, inflammation, and cellular signaling pathways. Despite challenges like short plasma half-life and complex regulatory mechanisms, rTFPI remains a promising candidate for modulating thrombotic and inflammatory disorders, reflecting the growing interest in precision anticoagulation therapies.
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