| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FTH |
| Uniprot No | P02794 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-183aa |
| 氨基酸序列 | TTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES |
| 预测分子量 | 48.1 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FTH(Ferritin Heavy Chain)重组蛋白的虚构参考文献示例，内容基于领域常见研究方向整理：
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1. **标题**: *Recombinant FTH as a Nanocarrier for Targeted Drug Delivery in Breast Cancer*
**作者**: Li, X., et al.
**摘要**: 本研究利用重组FTH蛋白的自组装特性，开发了一种靶向肿瘤的纳米药物载体。实验表明，该载体能高效负载化疗药物阿霉素，并通过肿瘤微环境响应性释放，显著抑制小鼠模型中乳腺癌细胞的生长，同时降低全身毒性。
2. **标题**: *FTH1 Recombinant Protein Modulates Iron Homeostasis in Neurodegenerative Disorders*
**作者**: Smith, J., & Chen, R.
**摘要**: 通过体外和阿尔茨海默病模型实验，发现重组FTH蛋白可有效调节脑部铁代谢异常，减少氧化应激和神经元损伤，为神经退行性疾病的铁螯合治疗提供了新策略。
3. **标题**: *Structural and Functional Analysis of Engineered FTH Mutants for Enhanced Iron Storage*
**作者**: Kim, S., et al.
**摘要**: 通过基因工程改造FTH蛋白的疏水核心，解析其晶体结构并证明突变体铁结合能力提升2.3倍，为开发高效铁离子吸附剂或生物传感器奠定基础。
4. **标题**: *FTH-Based Gene Therapy Vector for Liver-Specific Iron Overload Treatment*
**作者**: Gonzalez, M., et al.
**摘要**: 构建重组FTH与腺相关病毒(AAV)的融合载体，实现肝脏特异性递送。在遗传性血色素沉着症模型中，该疗法显著降低肝脏铁沉积，改善肝功能指标。
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注：以上文献为模拟示例，实际研究中需查询具体数据库(如PubMed)获取真实文献。
**Background of FTH Recombinant Protein**
Ferritin heavy chain (FTH) is a key subunit of the iron-storage protein ferritin, which plays a critical role in cellular iron homeostasis. It facilitates iron sequestration, preventing oxidative damage caused by free iron through the Fenton reaction. FTH exhibits ferroxidase activity, converting toxic Fe²⁺ into less reactive Fe³⁺ for safe storage within the ferritin nanocage. Dysregulation of FTH is linked to iron-related disorders, neurodegenerative diseases, and cancer, highlighting its physiological and pathological significance.
Recombinant FTH protein is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian systems. Its stable, self-assembling structure—a 24-mer nanocage—makes it a versatile platform in biotechnology. Researchers leverage FTH’s natural properties for applications such as targeted drug delivery, nanocarrier design, and vaccine development (e.g., antigen presentation). Its biocompatibility, uniform size, and modifiable surface enhance its utility in biomedical research.
Recent studies explore FTH’s role beyond iron metabolism, including immunomodulation and cellular stress responses. In cancer, FTH overexpression may promote tumor survival under oxidative stress, while its downregulation is associated with ferroptosis, a iron-dependent cell death pathway. Recombinant FTH also serves as a tool to study iron-handling mechanisms or develop diagnostics for iron-related diseases.
Overall, FTH recombinant protein bridges fundamental research and therapeutic innovation, offering insights into iron biology and enabling novel biomedical solutions. Its multifunctionality continues to drive interdisciplinary exploration in nanotechnology, oncology, and metabolic disease.
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