| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFXN2 |
| Uniprot No | Q96NB2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322 aa |
| 活性数据 | MEADLSGFNIDAPRWDQRTFLGRVKHFLNITDPRTVFVSERELDWAKVMVEKSRMGVVPPGTQVEQLLYAKKLYDSAFHPDTGEKMNVIGRMSFQLPGGMIITGFMLQFYRTMPAVIFWQWVNQSFNALVNYTNRNAASPTSVRQMALSYFTATTTAVATAVGMNMLTKKAPPLVGRWVPFAAVAAANCVNIPMMRQQELIKGICVKDRNENEIGHSRRAAAIGITQVVISRITMSAPGMILLPVIMERLEKLHFMQKVKVLHAPLQVMLSGCFLIFMVPVACGLFPQKCELPVSYLEPKLQDTIKAKYGELEPYVYFNKGL |
| 分子量 | 62.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人SFXN2蛋白的参考文献示例(注：文献为虚构，仅作格式参考)：
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1. **文献名称**：SFXN2 is a mitochondrial serine transporter involved in one-carbon metabolism
**作者**：Kory N. et al.
**摘要**：本研究通过生化实验和结构分析，鉴定SFXN2为线粒体内膜的丝氨酸转运蛋白，揭示其在细胞内一碳代谢中的关键作用，为癌症代谢研究提供新靶点。
2. **文献名称**：SFXN2 regulates iron-sulfur cluster biogenesis via interaction with mitochondrial cysteine desulfurase
**作者**：Chen X. et al.
**摘要**：SFXN2与线粒体铁硫簇组装关键酶NFS1互作，调控其稳定性及活性，缺失SFXN2导致细胞铁代谢异常及线粒体功能障碍。
3. **文献名称**：Loss of SFXN2 causes mitochondrial fragmentation and oxidative stress in mammalian cells
**作者**：Al-Mehdi A. et al.
**摘要**：通过CRISPR技术敲除SFXN2.发现其缺失引发线粒体形态异常、ROS累积及细胞凋亡增加，表明SFXN2对维持线粒体稳态至关重要。
4. **文献名称**：Structural basis of SFXN2-mediated serine transport across the mitochondrial inner membrane
**作者**：Wang Y. et al.
**摘要**：利用冷冻电镜解析重组人SFXN2蛋白的三维结构，阐明其转运丝氨酸的分子机制，为设计靶向药物提供结构基础。
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以上示例展示了文献的典型结构，实际研究中需根据具体论文内容调整。建议通过PubMed或Web of Science查询真实文献。
Sideroflexin 2 (SFXN2) is a member of the evolutionarily conserved sideroflexin protein family, which comprises five homologs (SFXN1-5) in humans. As an integral mitochondrial membrane protein, SFXN2 is implicated in metabolic transport and mitochondrial homeostasis. Though its precise molecular function remains under investigation, studies suggest its involvement in serine metabolism, iron-sulfur (Fe-S) cluster biosynthesis, and heme regulation—critical pathways for energy production, redox balance, and cellular proliferation.
Structurally, SFXN2 contains multiple transmembrane domains and a conserved sideroflexin motif, though its substrate specificity and transport mechanisms are not fully elucidated. Unlike SFXN1. which associates with mitochondrial complex II, SFXN2 may interact with enzymes in one-carbon metabolism, linking it to nucleotide synthesis and epigenetic regulation. Emerging evidence also highlights its role in apoptosis and cell cycle control, with dysregulated SFXN2 expression observed in cancers and neurodegenerative disorders. For instance, SFXN2 depletion impairs mitochondrial respiration and Fe-S-dependent enzyme activity, potentially contributing to pathologies like Parkinson’s disease.
Despite progress, SFXN2's exact biological roles and regulatory networks require further exploration. Current research leverages knockout models and interactome studies to clarify its contributions to mitochondrial physiology and disease mechanisms.
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