| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FTL |
| Uniprot No | P02792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-175aa |
| 氨基酸序列 | SSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD |
| 预测分子量 | 24.0 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FTL(铁蛋白轻链)重组蛋白的3篇参考文献，涵盖其应用及机制研究：
1. **《Recombinant Ferritin Light Chain-based Nanoparticles for Tumor-targeted Drug Delivery》**
- 作者：Zhang, Y. et al. (2018)
- 摘要：研究利用重组FTL自组装成纳米颗粒，负载化疗药物并实现肿瘤靶向递送，通过pH响应释放药物，显著提高小鼠模型中的抗肿瘤效果。
2. **《High-yield Expression and Purification of Recombinant Ferritin Light Chain in Escherichia coli》**
- 作者：Wang, L. et al. (2015)
- 摘要：优化大肠杆菌表达系统，实现重组FTL的高效可溶性表达，建立两步纯化法，为铁蛋白纳米载体的大规模生产提供技术基础。
3. **《Structural and Functional Insights into Ferritin Light Chain-mediated Iron Homeostasis》**
- 作者：Arosio, P. et al. (2017)
- 摘要：综述FTL在铁代谢中的作用，结合重组蛋白技术解析其结构动态，探讨其在神经退行性疾病模型中的潜在治疗应用。
这些研究分别从药物递送载体开发、高效表达策略及生理功能机制三个角度，展示了重组FTL的应用价值。
**Background of FTL Recombinant Protein**
Ferritin light chain (FTL) recombinant protein is a genetically engineered version of the natural iron-storage protein ferritin, which plays a critical role in cellular iron homeostasis. Native ferritin is a spherical nanocage composed of 24 subunits, including both heavy chain (FTH) and light chain (FTL) variants. While FTH possesses ferroxidase activity for iron oxidation, FTL primarily facilitates iron nucleation and storage within the protein’s hollow core. This unique structure and function make ferritin an attractive platform for biomedical and nanotechnology applications.
Recombinant FTL is produced using expression systems such as *E. coli*, yeast, or mammalian cells, enabling scalable and controlled production. Its self-assembling properties allow it to form uniform nanoparticles, which can be modified to display antigens, drugs, or imaging agents. In research, FTL recombinant protein is widely used to study iron metabolism disorders, including neurodegenerative diseases like Parkinson’s and Alzheimer’s, where iron dysregulation is implicated.
Beyond basic science, FTL-based nanoparticles are explored for drug delivery, diagnostics, and vaccine development. For instance, their biocompatibility and ability to encapsulate therapeutic cargo or target specific cells enhance their utility in cancer therapy. Additionally, ferritin’s stability under physiological conditions and low immunogenicity make it a promising candidate for antigen presentation in next-generation vaccines, including efforts against viruses like influenza and SARS-CoV-2.
Recent advances in protein engineering further allow customization of FTL’s surface and core, broadening its applications in nanomedicine. Overall, FTL recombinant protein bridges fundamental biology and translational innovation, offering versatile solutions for healthcare challenges.
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