| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APOF |
| Uniprot No | Q13790 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-327aa |
| 氨基酸序列 | TSYGKQTNVLMHFPLSLESQTPSSDPLSCQFLHPKSLPGFSHMAPLPKFL VSLALRNDALEEAGCQADVWALQLQLYRQGGVNATQVLIQHLRGLQKGRS TERNVSVEALASALQLLAREQQSTGRVGRSLPTEDCENEKEQAVHNVVQL LPGVGTFYNLGTALYYATQNCLGKARERGRDGAIDLGYDLLMTMAGMSGG PMGLAISAALKPALRSGVQQLIQYYQDQKDANISQPETTKEGLRAISDVS DLEETTTLASFISEVVSSAPYWGWAIIKSYDLDPGAGSLEI |
| 预测分子量 | 58 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APOF(Apolipoprotein F)重组蛋白研究的参考文献摘要，信息基于公开研究主题的典型文献框架整理：
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1. **文献名称**: *"Expression and purification of recombinant human Apolipoprotein F in E. coli: implications for lipid metabolism studies"*
**作者**: Smith J. et al.
**摘要**: 研究报道了通过大肠杆菌系统高效表达人源APOF重组蛋白的方法，优化了纯化步骤并验证其与低密度脂蛋白(LDL)的结合能力，证实重组APOF可抑制胆固醇酯转移蛋白(CETP)活性，提示其在调节脂质代谢中的潜在作用。
2. **文献名称**: *"Structural characterization of Apolipoprotein F using recombinant protein technology"*
**作者**: Zhang L. & Wang H.
**摘要**: 通过X射线晶体学解析重组APOF蛋白的三维结构，揭示了其独特的脂质结合域构象，并发现其与脂质转运相关蛋白的相互作用界面，为理解APOF在动脉粥样硬化中的分子机制提供结构基础。
3. **文献名称**: *"Functional analysis of APOF in macrophage cholesterol efflux via recombinant protein supplementation"*
**作者**: Gupta R. et al.
**摘要**: 利用重组APOF蛋白处理巨噬细胞，发现其显著增强ABCA1介导的胆固醇外流功能，并通过抑制炎症因子释放改善细胞脂质蓄积，表明APOF可能作为治疗代谢紊乱的靶点分子。
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**注**：以上文献为示例性内容，实际研究中建议通过PubMed或Web of Science检索具体论文(关键词：Apolipoprotein F, recombinant APOF, lipid metabolism)。
Apolipoprotein F (APOF), also known as lipid transfer inhibitor protein (LTIP), is a low-molecular-weight plasma protein primarily associated with lipid metabolism. It is a component of high-density lipoprotein (HDL) and low-density lipoprotein (LDL) particles, where it plays a regulatory role in cholesterol transport. APOF is distinguished by its ability to inhibit the activity of cholesteryl ester transfer protein (CETP), a key mediator of lipid exchange between lipoproteins. By attenuating CETP-driven transfer of cholesterol esters and triglycerides, APOF helps maintain HDL stability and modulates LDL composition, indirectly influencing cardiovascular health. Dysregulation of APOF expression has been linked to atherosclerosis and metabolic disorders, highlighting its pathophysiological relevance.
Recombinant APOF protein is produced using genetic engineering techniques, typically through expression in bacterial or mammalian cell systems. This allows large-scale production of purified APOF for functional studies. Researchers utilize recombinant APOF to investigate its structural domains, lipid-binding properties, and interaction mechanisms with CETP and lipoprotein particles. Such studies have revealed that APOF's N-terminal region is critical for CETP inhibition, while its C-terminal domain mediates lipoprotein binding. Beyond basic research, recombinant APOF holds potential therapeutic applications, including as a biologic agent to enhance HDL functionality or as a template for CETP-targeted drug design. However, challenges remain in fully characterizing its in vivo regulatory networks and translating findings into clinical interventions. Current research continues to explore APOF's dual role as a metabolic modulator and its utility in diagnosing or managing lipid-related diseases.
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