| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TF |
| 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. |
以下是关于组织因子(Tissue Factor, TF)重组蛋白的3-4篇参考文献，涵盖表达、结构及应用研究：
1. **文献名称**：*"Role of tissue factor in coagulation and hemostasis"*
**作者**：Morrissey, J.H. et al.
**摘要**：该研究探讨了重组TF在体外凝血机制中的作用，证实其作为凝血因子VIIa的辅因子，对激活凝血级联反应至关重要。
2. **文献名称**：*"Expression and characterization of recombinant human tissue factor in mammalian cells"*
**作者**：Rehemtulla, A. et al.
**摘要**：报道了在哺乳动物细胞系中高效表达功能性重组TF的方法，为后续研究其结构与功能提供了可靠来源。
3. **文献名称**：*"Crystal structure of the complex between tissue factor and factor VIIa"*
**作者**：Banner, D.W. et al.
**摘要**：通过X射线晶体学解析了TF与凝血因子VIIa的复合物三维结构，揭示了二者相互作用的分子机制，为抗凝药物设计奠定基础。
4. **文献名称**：*"Procoagulant activity of recombinant human tissue factor in animal models"*
**作者**：Dickneite, G. et al.
**摘要**：评估了重组TF在动物模型中的止血效果，证明其作为局部止血剂在创伤和手术中的潜在应用价值。
以上文献分别从功能机制、表达技术、结构解析及临床应用角度概括了TF重组蛋白的研究进展。
**Background of Recombinant TF Proteins**
Transcription factor (TF) recombinant proteins are engineered molecules designed to mimic or modulate the activity of natural transcription factors, which are critical regulators of gene expression. TFs bind to specific DNA sequences, enabling the activation or repression of target genes, thereby influencing cellular processes such as differentiation, proliferation, and apoptosis. Dysregulation of TFs is linked to diseases like cancer, autoimmune disorders, and developmental abnormalities.
The development of recombinant TF proteins leverages advances in molecular biology and protein engineering. Using recombinant DNA technology, genes encoding TFs are cloned into expression vectors and produced in host systems (e.g., *E. coli*, yeast, or mammalian cells). Purification techniques yield highly specific, functional proteins. These recombinant TFs retain DNA-binding domains and functional motifs, enabling their use in research and therapy.
Applications include drug discovery, where recombinant TFs serve as tools to study gene regulatory networks or as therapeutic agents to correct aberrant gene expression. For example, engineered zinc-finger or CRISPR-based TFs are explored for targeted gene editing. Additionally, recombinant TFs are utilized in biomanufacturing to control synthetic gene circuits or enhance protein production in cell cultures.
Challenges include maintaining protein stability, ensuring proper post-translational modifications (e.g., phosphorylation), and achieving cell-specific delivery *in vivo*. Innovations in protein engineering, such as fusion tags or nanocarriers, address these limitations. Overall, recombinant TF proteins represent a versatile platform for both basic research and translational medicine, bridging the gap between genomic insights and therapeutic interventions.
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