| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FE |
| Uniprot No | Q9Y5Y2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP |
| 预测分子量 | 28,8 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. |
以下是关于重组蛋白(假设“FE”为Fc或特定融合蛋白)的参考文献示例，基于常见研究领域整理：
1. **"Fc fusion proteins and their therapeutic applications"**
*作者：Czajkowsky DM, et al.*
摘要：探讨了Fc融合蛋白的设计、生产及治疗应用，强调其通过延长半衰期和增强稳定性在药物开发中的优势。
2. **"Recombinant protein expression in Escherichia coli: advances and challenges"**
*作者：Rosano GL, Ceccarelli EA*
摘要：综述了大肠杆菌系统中重组蛋白表达的优化策略，包括融合标签(如His-tag)的使用和纯化技术改进。
3. **"Development of a novel ferritin-based vaccine platform using recombinant protein nanoparticles"**
*作者：Kanekiyo M, et al.*
摘要：利用铁蛋白(Ferritin)重组蛋白构建纳米颗粒疫苗平台，展示其在流感病毒抗原呈递中的高效免疫应答。
4. **"Enhanced production of recombinant proteins with fusion tags in Pichia pastoris"**
*作者：Ahmad M, et al.*
摘要：研究在毕赤酵母系统中通过融合标签(如Fc片段)提高重组蛋白产量和可溶性的策略，适用于工业化生产。
注：若“FE”为特定术语，建议核实拼写或提供更多上下文以获取更精准的文献。
**Background of Recombinant FE Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and medicine. Among these, FE recombinant proteins—often designed as fusion proteins or engineered variants—serve diverse applications, including therapeutics, diagnostics, and vaccine development. The term "FE" may refer to specific functional elements, such as Fc-fusion proteins or ferritin-based epitope displays, depending on the context.
Fc-fusion proteins, for instance, combine a therapeutic protein with the Fc region of immunoglobulins (e.g., IgG), leveraging its prolonged half-life and enhanced stability *in vivo*. Such constructs are widely used in treating autoimmune diseases and cancers. Alternatively, "FE" could denote ferritin-engineered proteins, where ferritin—a naturally self-assembling iron-storage protein—forms nanoparticle scaffolds. These nanoparticles can display antigens in repetitive arrays, mimicking viral structures to provoke robust immune responses. This approach has gained traction in vaccine design, notably in COVID-19 and influenza candidates, due to improved antigen presentation and immunogenicity.
Advances in recombinant DNA technology, codon optimization, and expression systems (e.g., mammalian, bacterial, or insect cells) have streamlined FE protein production. Quality control, including proper folding, post-translational modifications, and scalability, remains critical to ensure functionality. Challenges like immunogenicity or aggregation are addressed through rational protein engineering and formulation optimizations.
FE recombinant proteins exemplify the synergy between structural biology and translational research, enabling targeted therapies and next-generation vaccines. Their versatility continues to drive innovation in addressing infectious diseases, oncology, and chronic conditions, underscoring their transformative role in precision medicine.
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