| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fre |
| Uniprot No | P0AEN1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-233aa |
| 氨基酸序列 | TTLSCKVTSVEAITDTVYRVRIVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASEINLYAKAVMDRILKDHQIVVDIPHGEAWLRDDEERPMILIAGGTGFSYARSILLTALARNPNRDITIYWGGREEQHLYDLCELEALSLKHPGLQVVPVVEQPEAGWRGRTGTVLTAVLQDHGTLAEHDIYIAGRFEMAKIARDLFCSERNAREDRLFGDAFAFI |
| 预测分子量 | 30.1 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“Fre重组蛋白”的假设性参考文献示例，供参考(实际文献可能需要根据具体研究领域进一步检索)：
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1. **文献名称**: *Heterologous Expression and Functional Characterization of Fre1 Recombinant Protein in Saccharomyces cerevisiae*
**作者**: Johnson M, et al.
**摘要**: 研究报道了酿酒酵母中Fre1重组蛋白的异源表达，证实其在细胞膜铁离子还原中的关键作用，并分析其酶活性对金属稳态的影响。
2. **文献名称**: *Engineering Fre-like Ferric Reductases for Enhanced Bioremediation Applications*
**作者**: Chen L, Wang H.
**摘要**: 通过定向进化改造Fre家族重组蛋白，优化其对重金属离子的还原效率，验证其在环境污染修复中的潜在应用价值。
3. **文献名称**: *Crystal Structure and Mechanistic Study of a Fre Recombinase from Plasmid pXX1*
**作者**: Müller R, et al.
**摘要**: 解析了来源于质粒pXX1的Fre重组酶的晶体结构，阐明其催化DNA位点特异性重组的分子机制，为基因编辑工具开发提供依据。
4. **文献名称**: *High-Yield Production of Recombinant FRE Protein in E. coli and Its Role in Antioxidant Pathways*
**作者**: Gupta S, et al.
**摘要**: 优化了FRE重组蛋白在大肠杆菌中的可溶性表达条件，并证明其通过调节硫氧还蛋白系统参与氧化应激反应。
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**注意**：以上文献为模拟示例，实际研究中请通过学术数据库(如PubMed、Web of Science)以准确关键词(如“Fre recombinase”“Ferric reductase recombinant”)检索。若“Fre”指特定术语，建议提供更多背景信息以便精准查找。
**Background of Freestyle™ (Fre) Recombinant Proteins**
Freestyle™ recombinant proteins are a class of engineered proteins produced using the FreeStyle™ expression system, a platform developed for high-yield, transient protein production in mammalian cell cultures, particularly in HEK293 and CHO cells. This system is widely adopted in biotechnology and pharmaceutical research due to its ability to generate complex proteins with proper folding, post-translational modifications (e.g., glycosylation), and functional activity, closely mimicking native human proteins.
The demand for recombinant proteins has surged with advancements in therapeutic biologics, including monoclonal antibodies, vaccines, and enzyme replacements. Traditional systems like *E. coli* or yeast often fail to produce functional eukaryotic proteins requiring specific modifications. Mammalian systems, like FreeStyle™, address this gap by enabling scalable, suspension-cell cultures that optimize protein yield and quality. The technology integrates optimized media, transfection reagents, and culture conditions to streamline production without stable cell line development.
Freestyle™ recombinant proteins are pivotal in drug discovery, structural biology, and diagnostics. They serve as tools for studying protein-protein interactions, validating drug targets, or as reference standards in quality control. Their clinical relevance is highlighted in producing biologics like trastuzumab or COVID-19 spike proteins for vaccine development.
Overall, the FreeStyle™ system represents a critical innovation in recombinant protein technology, balancing speed, scalability, and biological fidelity to meet the growing needs of biomedical research and therapeutic development.
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