| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MFRN |
| Uniprot No | Q9NYZ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-338aa |
| 氨基酸序列 | MELRSGSVGSQAVARRMDGDSRDGGGGKDATGSEDYENLPTSASVSTHMTAGAMAGILEHSVMYPVDSVKTRMQSLSPDPKAQYTSIYGALKKIMRTEGFWRPLRGVNVMIMGAGPAHAMYFACYENMKRTLNDVFHHQGNSHLANGIAGSMATLLHDAVMNPAEVVKQRLQMYNSQHRSAISCIRTVWRTEGLGAFYRSYTTQLTMNIPFQSIHFITYEFLQEQVNPHRTYNPQSHIISGGLAGALAAAATTPLDVCKTLLNTQENVALSLANISGRLSGMANAFRTVYQLNGLAGYFKGIQARVIYQMPSTAISWSVYEFFKYFLTKRQLENRAPY |
| 预测分子量 | 37,3 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MFRN(线粒体铁蛋白，Mitochondrial Ferritin)重组蛋白研究的示例性参考文献(内容为模拟，供参考格式)：
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1. **文献名称**：*Recombinant Expression and Functional Characterization of Mitochondrial Ferritin in Iron Homeostasis*
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究通过大肠杆菌系统成功表达并纯化了重组MFRN蛋白，证实其具有铁离子结合能力，并发现其过表达可减少细胞质铁水平，提示其在调控线粒体铁稳态中的关键作用。
2. **文献名称**：*Structural Insights into Mitochondrial Ferritin Oligomerization via Cryo-EM Analysis*
**作者**：Zhang R, Ito S, et al.
**摘要**：利用冷冻电镜解析了重组MFRN蛋白的高分辨率结构，揭示了其独特的24聚体组装模式，并发现其与胞质铁蛋白的结构差异，为理解其线粒体特异性功能提供依据。
3. **文献名称**：*MFRN Deficiency in Mice Induces Mitochondrial Dysfunction and Neurodegeneration*
**作者**：Gonzalez-Freire M, Arosio P, et al.
**摘要**：通过构建MFRN敲除小鼠模型，发现其线粒体铁超载和神经元损伤，重组MFRN蛋白治疗可部分逆转表型，表明其在神经退行性疾病中的潜在治疗价值。
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**注意**：以上为模拟文献，如需真实文献，建议通过PubMed、Web of Science等平台搜索关键词“Mitochondrial Ferritin recombinant”或“MFRN protein expression”获取最新研究。
**Background of Recombinant MFRN Protein**
Mitochondrial ferritin (MFt), encoded by the *FTMT* gene, is an iron-storage protein localized within mitochondria, distinct from cytosolic ferritin. It plays a critical role in regulating mitochondrial iron homeostasis by sequestering excess iron, thereby preventing oxidative damage caused by reactive oxygen species (ROS) generated via the Fenton reaction. MFt is particularly vital in tissues with high metabolic activity, such as the brain, heart, and skeletal muscle, where mitochondrial iron dysregulation is linked to neurodegenerative disorders, cardiomyopathy, and other pathologies.
Recombinant MFRN (MFt) protein is produced using genetic engineering techniques, typically expressed in bacterial or mammalian systems to ensure proper folding and post-translational modifications. Its structure mimics native MFt, featuring a 24-subunit spherical shell that binds and stores iron in a soluble, non-toxic form. This recombinant form enables precise study of MFt’s iron-binding kinetics, structural dynamics, and interactions with mitochondrial proteins involved in iron-sulfur cluster biogenesis and heme synthesis.
Research on recombinant MFt has advanced understanding of diseases like Friedreich’s ataxia, Alzheimer’s, and Parkinson’s, where mitochondrial iron overload exacerbates cellular dysfunction. It also serves as a tool for exploring therapeutic strategies, such as iron chelation or gene therapy, to restore iron balance. Additionally, recombinant MFt aids in drug screening and mechanistic studies, offering insights into its role in aging, metabolic disorders, and cancer. Its development underscores the growing emphasis on mitochondrial-targeted therapies to address iron-related pathologies.
In summary, recombinant MFRN protein is a pivotal tool for dissecting mitochondrial iron metabolism and developing interventions for diseases rooted in iron mishandling.
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