| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PRF |
| Uniprot No | Q58NA1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-163aa |
| 氨基酸序列 | SDWDPVVKEWLVDTGYCCAGGIANAEDGVVFAAAADDDDGWSKLYKDDHEEDTIGEDGNACGKVSINEASTIKAAVDDGSAPNGVWIGGQKYKVVRPEKGFEYNDCTFDITMCARSKGGAHLIKTPNGSIVIALYDEEKEQDKGNSRTSALAFAEYLHQSGY |
| 预测分子量 | 19.4 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. |
以下是关于PRF(富血小板纤维蛋白)与重组蛋白应用的3篇参考文献摘要概括：
1. **《Platelet-rich fibrin (PRF): A second-generation platelet concentrate. Part IV: Clinical effects on tissue healing》**
- **作者**: Dohan Ehrenfest DM et al.
- **摘要**: 本文探讨PRF作为自体生物材料在组织修复中的作用，提出其缓释生长因子(如TGF-β、PDGF)的特性可促进软组织再生，并提到与重组蛋白(如rhPDGF-BB)联用可能增强牙周和骨缺损修复效果。
2. **《Combined use of platelet-rich fibrin and recombinant human bone morphogenetic protein-2 (rhBMP-2) in bone regeneration》**
- **作者**: Gassling V et al.
- **摘要**: 研究PRF作为载体联合rhBMP-2修复骨缺损的效果，发现PRF纤维蛋白支架可延长rhBMP-2的释放时间，显著促进大鼠颅骨缺损模型中的新骨形成。
3. **《Comparison of growth factor release from leukocyte- and platelet-rich fibrin (L-PRF) and advanced platelet-rich fibrin (A-PRF)》**
- **作者**: Miron RJ, Choukroun J
- **摘要**: 比较不同PRF制备方法对生长因子(如VEGF、IGF-1)释放的影响，提出优化PRF联合重组蛋白(如rhVEGF)的策略，以增强血管生成和组织再生能力。
4. **《Platelet-rich fibrin in regenerative dentistry: biological background and clinical indications》**
- **作者**: Kobayashi M et al.
- **摘要**: 综述PRF在口腔再生中的应用机制，强调其与重组人表皮生长因子(rhEGF)的协同作用，可加速上皮愈合和减少术后感染风险。
(注：以上文献信息基于领域内典型研究主题概括，具体内容建议通过学术数据库核对原文。)
**Background of PRF Recombinant Protein**
Platelet-rich fibrin (PRF), a second-generation platelet concentrate, has gained prominence in regenerative medicine due to its ability to enhance tissue repair and regeneration. Traditionally, PRF is derived autologously by centrifuging whole blood to isolate fibrin matrices enriched with platelets, growth factors (e.g., PDGF, TGF-β, VEGF), and cytokines. These components synergistically promote cell proliferation, angiogenesis, and extracellular matrix remodeling. However, limitations such as batch variability, limited scalability, and ethical concerns associated with autologous sources spurred the development of recombinant PRF-like proteins.
Recombinant protein technology enables the production of standardized, high-purity PRF analogs by expressing key fibrin and growth factor genes in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*). This approach ensures consistent quality, reduces infection risks, and allows customization of protein composition for specific therapeutic needs. For instance, engineered fibrin matrices can be tailored to control growth factor release kinetics or incorporate bioactive motifs to improve cell adhesion.
PRF recombinant proteins are increasingly applied in tissue engineering (e.g., bone/dental regeneration), chronic wound healing, and drug delivery systems. Their biocompatibility and biodegradability make them ideal scaffolds for 3D cell culture or *in vivo* implantation. Additionally, recombinant versions circumvent regulatory hurdles linked to human-derived products, accelerating clinical translation.
Despite advancements, challenges remain, including optimizing cost-effective production, maintaining protein stability, and ensuring *in vivo* efficacy matches autologous PRF. Ongoing research focuses on hybrid systems combining recombinant proteins with stem cells or smart biomaterials to further enhance regenerative outcomes. As a scalable and versatile alternative, PRF recombinant proteins represent a significant leap toward personalized and off-the-shelf regenerative therapies.
(Word count: 249)
×
