| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | F3 |
| Uniprot No | P13726 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-295aa |
| 氨基酸序列 | METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS |
| 预测分子量 | 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F3(组织因子，Tissue Factor)重组蛋白的3篇代表性文献示例(注：文献为虚拟示例，仅供参考格式和内容框架)：
1. **文献名称**: *"Expression and functional characterization of recombinant human tissue factor in mammalian cells"*
**作者**: Smith J, et al.
**摘要**: 本研究通过哺乳动物表达系统成功制备了重组人F3蛋白，并验证其促凝血活性。结果表明，重组F3与天然蛋白结构一致，可与凝血因子VIIa结合并激活下游凝血级联反应。
2. **文献名称**: *"Structural analysis of recombinant F3 extracellular domain and its role in cancer-associated thrombosis"*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了重组F3胞外域的三维结构，揭示了其与磷脂膜相互作用的分子机制。实验进一步证明，肿瘤细胞分泌的重组F3可显著促进血栓形成，提示其在癌症并发症中的潜在作用。
3. **文献名称**: *"Development of a high-yield Escherichia coli system for recombinant F3 production"*
**作者**: Zhang R, et al.
**摘要**: 报道了一种优化的大肠杆菌表达体系，通过密码子优化和包涵体复性策略实现重组F3的高效可溶性表达，为大规模制备低成本F3蛋白提供了新方法。
**建议**：实际文献需通过PubMed、Web of Science等平台检索关键词(如“recombinant tissue factor”或“recombinant F3 protein”)，并结合具体研究方向筛选。
F3 recombinant protein is a synthetic peptide derived from the F3 peptide sequence, a fragment originally identified in human high-molecular-weight kininogen. The F3 peptide has gained attention for its tumor-homing properties, particularly its ability to selectively bind to nucleolin—a protein overexpressed on the surface of cancer cells and endothelial cells in tumor vasculature. This unique targeting capability has positioned F3 recombinant protein as a promising tool in cancer therapeutics and diagnostics.
Produced via recombinant DNA technology, the F3 protein is typically expressed in bacterial or mammalian systems, ensuring high purity and scalability. Its structure includes functional domains that facilitate cellular internalization, enabling it to deliver therapeutic payloads (e.g., drugs, siRNA, or imaging agents) directly to tumor cells. Studies highlight its role in inhibiting angiogenesis by disrupting nucleolin-mediated signaling pathways, thereby suppressing tumor growth and metastasis.
Research has expanded into applications beyond oncology, including anti-inflammatory therapies and regenerative medicine, owing to its interactions with extracellular matrix components. Current challenges include optimizing its pharmacokinetics and minimizing off-target effects, but advances in conjugation techniques and nanotechnology integration are addressing these limitations. The F3 recombinant protein exemplifies the convergence of molecular targeting and bioengineering, offering a versatile platform for precision medicine.
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