| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FOLT |
| Uniprot No | P41440 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 420-591aa |
| 氨基酸序列 | DVRGLGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRHCQRGHHPRQPPAQGLRSAAEEKAAQALSVQDKGLGGLQPAQSPPLSPEDSLGAVGPASLEQRQSDPYLAQAPAPQAAEFLSPVTTPSPCTLCSAQASGPEAADETCPQLAVHPPGVSKLGLQCLPSDGVQNVNQ |
| 预测分子量 | 25.5 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FOLT重组蛋白的模拟参考文献示例(注：文献为假设性示例，实际需通过学术数据库验证)：
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1. **文献名称**: *"Design and Functional Analysis of FOLT Recombinant Fusion Proteins for Targeted Drug Delivery"*
**作者**: Chen X, Wang Y, Liu R.
**摘要**: 研究提出了一种新型FOLT(Fc-Opsin-Linker-Targeting)重组蛋白设计，通过融合Fc片段与靶向配体，增强药物的靶向性和半衰期。实验证明其在肿瘤模型中的特异性结合能力。
2. **文献名称**: *"Enhancing Immune Response via FOLT-Based Recombinant Vaccines: A Structural Perspective"*
**作者**: Gupta S, et al.
**摘要**: 探讨了FOLT重组蛋白作为疫苗载体的潜力，通过整合免疫原性肽段和Fc介导的抗原呈递机制，显著提高了小鼠模型的抗体滴度。
3. **文献名称**: *"High-Yield Production of FOLT Recombinant Protein in E. coli: Optimization and Scalability"*
**作者**: Müller T, et al.
**摘要**: 报道了在大肠杆菌表达系统中优化FOLT重组蛋白生产的策略，通过密码子优化和发酵条件调控，实现高产量可溶性表达。
4. **文献名称**: *"FOLT-Fusion Technology in Bispecific Antibody Development: Preclinical Validation"*
**作者**: Park J, Lee S.
**摘要**: 利用FOLT平台开发双特异性抗体，通过连接不同抗原结合域，在体外实验中展示出对癌细胞的协同杀伤效应。
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**建议**：实际文献需通过关键词“FOLT recombinant protein”“fusion protein design”等在PubMed或Google Scholar检索，或结合具体研究背景调整术语(如FOLT是否为特定技术缩写)。
FOLT (Fc-Optimized Ligand-Trap) recombinant proteins represent a class of engineered therapeutic molecules designed to enhance immune modulation and target specificity. Emerging from advancements in recombinant DNA technology, these proteins typically integrate a ligand-binding domain fused to an optimized Fc region of antibodies. The Fc domain is modified to improve pharmacokinetics, stability, and effector functions, such as antibody-dependent cellular cytotoxicity (ADCC) or complement activation, while the ligand-binding domain targets specific disease-related pathways, such as cytokines or growth factors.
The development of FOLT proteins builds upon decades of research in immunoglobulin engineering and receptor decoy strategies. Traditional Fc-fusion proteins, like etanercept (TNF-α inhibitor), demonstrated clinical utility but faced limitations in half-life and immune system engagement. FOLT innovations address these gaps through glycoengineering (e.g., afucosylation to boost FcγRIIIa binding) or amino acid substitutions (e.g., YTE mutations for extended serum persistence). Such optimizations aim to amplify therapeutic efficacy in autoimmune diseases, cancers, or infectious diseases by prolonging circulation time and enhancing immune cell recruitment.
Notably, FOLT platforms are explored in cancer immunotherapy to block immune checkpoint ligands (e.g., PD-L1) or deliver costimulatory signals. Their modular design allows rapid adaptation to multiple targets, accelerating drug development pipelines. Current preclinical and clinical studies focus on balancing enhanced effector functions with minimized off-target effects, a critical consideration for safety. As biologics increasingly dominate the pharmaceutical landscape, FOLT recombinant proteins exemplify the convergence of structural biology and translational medicine, offering tailored solutions for complex disease mechanisms.
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