| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ftnA |
| Uniprot No | P52093 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-167aa |
| 氨基酸序列 | MLSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAKKLIVFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKGKDHATFNFLQWYVSEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIAKSRKS |
| 预测分子量 | 21.8 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ftnA重组蛋白的3篇参考文献示例(注：文献为虚拟示例，仅供格式参考)：
1. **文献名称**: "Heterologous expression and functional characterization of recombinant ftnA in Salmonella typhimurium"
**作者**: Müller, J. et al.
**摘要**: 研究报道了通过原核表达系统成功表达ftnA重组蛋白，并证实其参与沙门氏菌铁离子存储过程，通过铁螯合实验证明重组ftnA可显著增强细菌在缺铁环境下的存活率。
2. **文献名称**: "Crystal structure analysis of ftnA recombinant protein reveals novel iron-binding motifs"
**作者**: Tanaka, K. & Chen, W.
**摘要**: 通过X射线晶体学解析了ftnA重组蛋白的三维结构，发现其具有独特的24聚体笼状结构，并鉴定出两个新的铁离子结合位点，为理解细菌铁代谢机制提供结构基础。
3. **文献名称**: "Recombinant ftnA as a molecular marker for bacterial oxidative stress response"
**作者**: Gupta, R. et al.
**摘要**: 利用重组ftnA蛋白进行功能研究，发现其能够通过调控活性氧(ROS)水平保护大肠杆菌免受氧化损伤，提示ftnA在细菌应激应答中的双重作用(铁存储与抗氧化)。
4. **文献名称**: "High-yield production of ftnA recombinant protein using Pichia pastoris expression system"
**作者**: Li, Y. et al.
**摘要**: 开发了基于毕赤酵母的真核表达体系，实现ftnA重组蛋白的高效分泌表达(产量达120 mg/L)，并通过动态光散射验证其均一性，为大规模制备诊断用抗原奠定基础。
The ftnA gene encodes a ferritin-like protein, primarily known for its role in iron storage and detoxification across prokaryotic and eukaryotic organisms. As a member of the ferritin superfamily, FtnA forms a hollow, spherical nanocage structure composed of 24 subunits, capable of sequestering excess intracellular iron in a non-toxic, bioavailable form. This protein plays a critical role in maintaining iron homeostasis by oxidizing Fe²⁺ to Fe³⁺ via its ferroxidase center, facilitating iron mineralization within its core.
Recombinant FtnA proteins are engineered through heterologous expression systems (e.g., E. coli) for structural and functional studies. Its self-assembling properties, stability, and biocompatibility have attracted interest in nanotechnology and biomedicine. For instance, FtnA’s cavity can encapsulate therapeutic agents or imaging probes, making it a promising drug delivery vehicle. Additionally, its surface can be genetically or chemically modified for targeted applications.
In bacterial pathogens like *Salmonella* or *Helicobacter pylori*, FtnA contributes to virulence by mitigating host-induced oxidative stress. Research on recombinant FtnA aids in understanding microbial resistance mechanisms and developing antimicrobial strategies. Moreover, its similarity to human ferritin enables cross-species studies on iron-related disorders, such as anemia or neurodegenerative diseases.
Recent advances in protein engineering have optimized FtnA’s iron-loading efficiency and thermal stability, expanding its utility in industrial biocatalysis and environmental remediation (e.g., heavy metal adsorption). Despite its versatility, challenges remain in scaling production and ensuring conformational uniformity for clinical applications. Ongoing research focuses on tailoring FtnA-based platforms for vaccines, diagnostics, and smart nanomaterials, underscoring its multifaceted potential in biotechnology.
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