| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ffp |
| Uniprot No | Q9F4F7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-224aa |
| 氨基酸序列 | MKIYGIYMDRPLSQEETDRLMSFVSAEKREKCRRFYHKEDAHRTLLGDVLVRSVISEQYQLNKADIRFSAQEYGKPCIPDLPNAHFNISHSGHWVIGAFDSDPIGVDIEKMKPISLGIAERFFSKNEYSDLLSKHKDEQNDYFYHLWSMKESFIKQEGKGLSLPLDSFSVRLHEDGRVSVELPEHHTPCFIKTYEVDPGYKMAVCAARPDFPEDITMISYEALL |
| 预测分子量 | 25,9 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FFP重组蛋白的3篇示例参考文献(注：文献为虚构，仅用于示例)：
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1. **文献名称**：*Optimization of FFP-Recombinant Protein Expression in Pichia pastoris for Industrial Applications*
**作者**：Zhang et al.
**摘要**：研究通过改造毕赤酵母表达系统，利用FFP(Fusion Facilitated Purification)技术提高重组蛋白的分泌效率，显著降低了纯化成本并提升产量，为工业化生产提供了新策略。
2. **文献名称**：*FFP-Tagged Recombinant Cytokines Enhance Stability in Serum-Free Formulations*
**作者**：Thompson & Garcia
**摘要**：开发了一种基于FFP标签的重组细胞因子，证明其在不含血清的培养条件下仍保持高稳定性和生物活性，为生物制药开发提供了改良方案。
3. **文献名称**：*Mechanistic Insights into FFP-Mediated Protein Folding in Mammalian Cells*
**作者**：Kumar et al.
**摘要**：通过分子动力学模拟和实验验证，揭示了FFP伴侣蛋白在哺乳动物细胞中促进重组蛋白正确折叠的作用机制，为治疗性蛋白生产优化奠定基础。
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以上示例参考了重组蛋白表达优化、稳定性增强及折叠机制等典型研究方向，FFP被设定为一种虚构的蛋白标签或辅助技术。实际研究中建议通过学术数据库(如PubMed、ScienceDirect)检索具体关键词获取真实文献。
**Background of FFP Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine. Among these, Fc fusion proteins (FFPs) represent a specialized class designed by fusing a target protein (e.g., a receptor, enzyme, or antigen) to the Fc region of an immunoglobulin (IgG). This hybrid structure leverages the beneficial properties of antibodies, such as prolonged serum half-life and enhanced stability, while retaining the functional activity of the fused protein.
The concept emerged in the 1980s, driven by advances in molecular cloning and protein engineering. Early successes, such as etanercept (a TNF-α receptor-Fc fusion for autoimmune diseases), demonstrated FFPs' therapeutic potential. By exploiting the neonatal Fc receptor (FcRn) recycling mechanism, FFPs achieve extended circulation time, reducing dosing frequency compared to non-fused counterparts. Additionally, the Fc domain facilitates purification via Protein A/G affinity chromatography, streamlining manufacturing.
FFPs are widely used in therapeutics, vaccines, and diagnostics. In therapeutics, they target cytokines (e.g., IL-1. VEGF) or immune checkpoints (e.g., CTLA-4), offering tailored treatments for cancer, autoimmune disorders, and infectious diseases. As vaccines, Fc-fused antigens enhance immunogenicity by promoting dendritic cell uptake via Fcγ receptors. In diagnostics, FFPs serve as detection reagents due to their stability and binding specificity.
Challenges include optimizing fusion design to avoid steric hindrance, mitigating immunogenicity risks, and ensuring cost-effective production. Recent innovations, such as modular Fc platforms and glycoengineering, aim to enhance functionality and scalability.
Overall, FFPs exemplify the synergy between antibody biology and recombinant technology, bridging therapeutic efficacy with practical manufacturability. Their continued evolution aligns with the growing demand for precision biologics in global healthcare.
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