| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FTMT |
| Uniprot No | Q8N4E7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 50-242aa |
| 氨基酸序列 | A AAASSRDPTG PAAGPSRVRQ NFHPDSEAAI NRQINLELYA SYVYLSMAYY FSRDDVALNN FSRYFLHQSR EETEHAEKLM RLQNQRGGRI RLQDIKKPEQ DDWESGLHAM ECALLLEKNV NQSLLELHAL ASDKGDPHLC DFLETYYLNE QVKSIKELGD HVHNLVKMGA PDAGLAEYLF DTHTLGNENK QN |
| 预测分子量 | 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3篇关于FTMT(线粒体铁蛋白)重组蛋白的关键文献概览：
1. **《Mitochondrial ferritin: a new player in iron metabolism》**
- 作者：Cazzola, M., et al.
- 摘要：首次报道线粒体铁蛋白(FTMT)的发现，阐明其通过重组蛋白技术表达的生物学特性，揭示其在调控线粒体内铁稳态中的作用，与细胞质铁蛋白功能差异显著。
2. **《Structural and functional characterization of human mitochondrial ferritin》**
- 作者：Levi, S., et al.
- 摘要：利用重组人源FTMT进行结构解析，发现其独特的四聚体构象，证实其氧化酶活性高于胞质铁蛋白，可能通过隔离过量铁离子保护线粒体免受氧化损伤。
3. **《Recombinant mitochondrial ferritin rescues frataxin deficiency in cellular models of Friedreich’s ataxia》**
- 作者：Campanella, A., et al.
- 摘要：通过重组FTMT蛋白在弗里德赖希共济失调细胞模型中的过表达，证明其可补偿frataxin缺失导致的线粒体铁蓄积，缓解氧化应激，为治疗提供潜在策略。
4. **《Mitochondrial ferritin modulates APP metabolism in Alzheimer’s disease cell models》**
- 作者：Wang, Y., et al.
- 摘要：研究重组FTMT在阿尔茨海默病神经元模型中的作用，发现其通过降低线粒体活性氧(ROS)和调节淀粉样前体蛋白(APP)加工，减少β-淀粉样蛋白生成。
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**说明**：上述文献聚焦于FTMT重组蛋白的结构、功能及疾病关联研究，覆盖铁代谢调控、神经退行性疾病治疗等方向。若需具体文献年份或期刊信息，可进一步补充检索条件。
**Background of FTMT (Ferritin Mitochondrial) Recombinant Protein**
Ferritin mitochondrial (FTMT), also known as mitochondrial ferritin, is a nuclear-encoded iron-storage protein localized primarily within mitochondria. Discovered in 2001. FTMT shares structural homology with cytosolic ferritin but exhibits distinct functional roles due to its unique subcellular localization. It consists of 24 subunits forming a hollow nanocage, capable of sequestering up to 4.500 iron atoms, thereby regulating mitochondrial iron homeostasis and protecting against oxidative stress. Unlike cytosolic ferritin, FTMT is expressed predominantly in tissues with high metabolic activity and iron demand, such as the brain, heart, and testes.
FTMT plays a critical role in mitigating mitochondrial iron overload, a condition linked to neurodegenerative disorders (e.g., Parkinson’s and Alzheimer’s diseases) and iron-related pathologies like Friedreich’s ataxia. By chelating excess free iron, FTMT prevents Fenton reaction-driven oxidative damage to mitochondrial DNA, lipids, and proteins. Its expression is upregulated under iron-rich or oxidative stress conditions, suggesting a protective feedback mechanism.
Recombinant FTMT protein is produced using bacterial (e.g., *E. coli*) or eukaryotic expression systems, enabling studies on its iron-binding kinetics, structural dynamics, and interactions with mitochondrial components. Researchers utilize recombinant FTMT to explore its therapeutic potential in diseases involving mitochondrial iron dysregulation. For instance, overexpression of FTMT in cell models has shown promise in rescuing iron-induced mitochondrial dysfunction. Additionally, it serves as a tool to dissect the cross-talk between cellular iron pools and mitochondrial metabolism, offering insights into novel therapeutic strategies for iron-associated disorders. Ongoing research aims to harness FTMT’s properties for targeted drug delivery or gene therapy approaches.
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