| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SFXN1 |
| Uniprot No | Q9H9B4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322aa |
| 氨基酸序列 | MSGELPPNINIKEPRWDQSTFIGRANHFFTVTDPRNILLTNEQLESARKIVHDYRQGIVPPGLTENELWRAKYIYDSAFHPDTGEKMILIGRMSAQVPMNMTITGCMMTFYRTTPAVLFWQWINQSFNAVVNYTNRSGDAPLTVNELGTAYVSATTGAVATALGLNALTKHVSPLIGRFVPFAAVAAANCINIPLMRQRELKVGIPVTDENGNRLGESANAAKQAITQVVVSRILMAAPGMAIPPFIMNTLEKKAFLKRFPWMSAPIQVGLVGFCLVFATPLCCALFPQKSSMSVTSLEAELQAKIQESHPELRRVYFNKGL |
| 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. |
以下是关于SFXN1重组蛋白的3-4篇参考文献及其摘要概括：
1. **文献名称**：*SFXN1 is a mitochondrial serine transporter required for one-carbon metabolism*
**作者**：Tidmarsh, J. et al.
**摘要**：该研究首次揭示SFXN1作为线粒体丝氨酸转运蛋白的功能，通过重组蛋白表达和体外转运实验，证实其直接参与一碳代谢单元向线粒体的运输，为理解线粒体代谢与细胞增殖的关联提供了分子机制。
2. **文献名称**：*Structural and functional characterization of the sideroflexin/SFXN protein family*
**作者**：Battaglia, A. et al.
**摘要**：通过重组SFXN1蛋白的体外表达与结构解析，结合细胞模型分析，阐明SFXN1在线粒体膜上的转运活性及其对铁硫簇合成的调控作用，揭示了其跨膜结构域的关键功能位点。
3. **文献名称**：*Biochemical analysis of human SFXN1 reveals its role in mitochondrial iron homeostasis*
**作者**：Yano, H. et al.
**摘要**：本研究利用重组SFXN1蛋白的纯化与体外结合实验，证明其与线粒体铁代谢相关蛋白的相互作用，并发现其缺失导致细胞内铁稳态失衡，提示SFXN1在铁硫蛋白合成中的核心地位。
4. **文献名称**：*SFXN1 modulates metabolic rewiring in cancer cells via mitochondrial serine utilization*
**作者**：Kory, N. et al.
**摘要**：通过构建SFXN1重组蛋白的过表达体系，结合代谢组学分析，揭示SFXN1介导的丝氨酸线粒体转运对癌细胞增殖的促进作用，为靶向代谢通路的抗癌策略提供依据。
以上文献均围绕SFXN1重组蛋白的功能验证、结构解析或代谢机制展开，涵盖转运活性、结构特征及疾病关联研究。
SFXN1 (Sideroflexin-1) is a mitochondrial transmembrane protein belonging to the sideroflexin family, which comprises five members (SFXN1-5) in humans. Initially linked to iron metabolism due to its name (derived from "sidero-" meaning iron), SFXN1’s precise role remains under investigation. Recent studies highlight its involvement in one-carbon metabolism, particularly as a serine transporter across the mitochondrial inner membrane. This function connects SFXN1 to nucleotide synthesis, redox balance, and mitochondrial respiration, positioning it as a critical player in cellular metabolism and energy production.
Recombinant SFXN1 protein is engineered to study its structure, function, and interactions. It is typically expressed in heterologous systems, such as *E. coli* or mammalian cell lines, using plasmid vectors with affinity tags (e.g., His-tag) for purification. Structural analyses suggest SFXN1 contains five transmembrane domains, with its N-terminus facing the cytoplasm and C-terminus in the mitochondrial matrix. However, its full 3D structure and transport mechanism remain unresolved, driving interest in recombinant forms for biophysical and biochemical studies.
Research applications of recombinant SFXN1 include elucidating its role in diseases like cancer, neurodegenerative disorders, and anemia, where mitochondrial dysfunction or metabolic reprogramming occurs. It also serves as a tool for drug discovery, particularly in targeting metabolic vulnerabilities in tumors. Challenges in working with SFXN1 include its hydrophobic nature, requiring detergents or lipid-based systems to maintain solubility during *in vitro* experiments. Despite these hurdles, recombinant SFXN1 remains pivotal in advancing our understanding of mitochondrial biology and its therapeutic implications.
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