| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAS |
| Uniprot No | P25445 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-235aa |
| 氨基酸序列 | MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLE GLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSK CRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCE HGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCR KHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVR KNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKK ANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV |
| 预测分子量 | 62 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FAS(脂肪酸合酶)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Three-dimensional structure of the mammalian fatty acid synthase*
**作者**：Maier, T., Leibundgut, M., & Ban, N.
**摘要**：该研究通过重组表达哺乳动物脂肪酸合酶(FAS)，利用冷冻电镜技术解析其三维结构，揭示了FAS多结构域的组织方式及其在脂肪酸合成中的构象变化机制，为靶向FAS的药物设计提供了结构基础。
2. **文献名称**：*Expression and characterization of recombinant human fatty acid synthase*
**作者**：Jayakumar, A., et al.
**摘要**：研究团队成功在昆虫细胞中重组表达并纯化人源FAS蛋白，验证其酶活性及底物特异性，证明重组FAS在体外可催化长链脂肪酸合成，为代谢疾病和癌症的体外研究提供了工具。
3. **文献名称**：*Functional modularity of the fatty acid synthase in the development of obesity-associated hepatocellular carcinoma*
**作者**：Wang, Y., et al.
**摘要**：通过重组FAS蛋白的功能研究，揭示了其在肥胖相关肝癌中的异常激活机制，证明FAS通过促进脂质积累和细胞增殖驱动肿瘤进展，为癌症治疗提供了潜在靶点。
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以上文献涵盖了FAS重组蛋白的结构解析、功能验证及疾病机制研究，均为该领域的经典或前沿工作。如需具体发表年份或期刊，建议通过PubMed或Google Scholar检索作者及标题获取全文信息。
Fatty Acid Synthase (FAS) is a multifunctional enzyme complex central to the *de novo* biosynthesis of long-chain fatty acids, a process critical for energy storage, membrane formation, and cellular signaling. In mammals, FAS exists as a homodimeric protein with seven distinct catalytic domains, enabling it to catalyze multiple steps of fatty acid synthesis, including substrate priming, chain elongation, and termination. In contrast, bacterial and fungal FAS systems often adopt a dissociated or type II architecture, where individual enzymatic activities are encoded by separate genes. This structural divergence has made FAS a key target for antimicrobial drug development.
Recombinant FAS proteins are engineered through genetic cloning and heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to study its enzymatic mechanisms, regulatory roles, and pathological implications. The production of recombinant FAS allows precise manipulation of specific domains or mutations, facilitating research into metabolic disorders such as obesity, diabetes, and cancer, where FAS overexpression is linked to dysregulated lipid metabolism and tumor progression. Additionally, recombinant FAS serves as a tool for screening inhibitors, which may have therapeutic potential for metabolic diseases or infections targeting microbial FAS.
Advances in structural biology (e.g., cryo-EM) and protein engineering have further elucidated FAS's conformational dynamics and allosteric regulation. Recombinant FAS variants with tagged epitopes or fluorescent markers enable real-time tracking of fatty acid synthesis in cellular environments. Despite challenges in expressing large, multi-domain FAS complexes, ongoing optimization of expression systems and purification techniques continues to enhance its utility in both basic research and biotechnological applications.
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