| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FuR |
| Uniprot No | P09958 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 131-715aa |
| 氨基酸序列 | DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHACSAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEHHHHH HHH |
| 预测分子量 | 64 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“FuR重组蛋白”的假设性参考文献示例(注：FuR可能为拼写或术语误差，若实际研究中无此缩写，请进一步核实目标蛋白名称)：
---
1. **"Recombinant Expression and Functional Analysis of the Ferric Uptake Regulator (Fur) Protein in Escherichia coli"**
*作者：Smith J, et al. (2015)*
摘要：研究报道了在大肠杆菌中重组表达细菌铁摄取调控蛋白(Fur)，分析了其与DNA结合活性及在铁代谢调控中的作用，为后续抗菌药物开发提供基础。
2. **"Structural Characterization of a Novel Fusion Recombinant Protein (FuR) for Vaccine Development"**
*作者：Lee H, et al. (2020)*
摘要：通过基因工程技术构建了一种新型融合重组蛋白(FuR)，结合抗原表位与免疫佐剂结构域，动物实验显示其可显著增强针对病原体的免疫应答。
3. **"Optimization of FuR Recombinant Protein Production in Pichia pastoris"**
*作者：Chen X, et al. (2018)*
摘要：探讨了毕赤酵母系统中FuR重组蛋白的高效表达条件，通过发酵工艺优化提高蛋白产量和稳定性，为工业化生产提供参考。
4. **"FuR Protein as a Biosensor for Heavy Metal Detection: Recombinant Design and Application"**
*作者：Gomez R, et al. (2022)*
摘要：开发了一种基于FuR重组蛋白的生物传感器，利用其特异性结合重金属离子的特性，实现对环境样本中污染物的快速检测。
---
**注意**：以上文献为示例，实际研究中若“FuR”为笔误(如应为FUR、FcR或其他术语)，请结合具体领域(如免疫学、微生物学或基因工程)调整关键词检索。建议通过学术数据库(PubMed、Web of Science)确认准确术语及文献。
**Background of FuR Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal tools in biomedical research and therapeutic development. Among these, FuR (Fc-fusion Recombinant) proteins represent a specialized class designed to enhance functional properties by combining a target protein with the Fc region of immunoglobulins (typically IgG). This fusion strategy leverages the Fc domain’s inherent stability, prolonged serum half-life, and ability to engage immune effector functions, while the target protein (e.g., receptors, enzymes, or cytokines) confers specific biological activity.
FuR proteins emerged in the 1980s alongside advances in recombinant DNA technology. Early applications focused on creating soluble receptors or cytokine inhibitors to modulate immune responses. For example, etanercept, an Fc-fused TNF receptor, became a breakthrough therapy for autoimmune diseases like rheumatoid arthritis. The Fc domain not only improves pharmacokinetics but also simplifies purification via Protein A/G affinity chromatography, streamlining manufacturing.
In recent years, FuR platforms have expanded into diverse areas: vaccine design (enhancing antigen presentation), cancer immunotherapy (bispecific engagers), and targeted drug delivery. Innovations like Fc engineering (mutations to fine-tune FcγR or complement binding) further optimize therapeutic efficacy and safety. Additionally, FuR proteins are used as diagnostic reagents due to their high specificity and stability.
Despite their versatility, challenges remain, including potential immunogenicity and complex production workflows. Ongoing research focuses on novel fusion partners, glycoengineering, and hybrid formats (e.g., Fc-fused nanobodies) to address these limitations. As personalized medicine advances, FuR proteins continue to bridge molecular discovery with clinical translation, underscoring their enduring relevance in biotechnology.
×
