| 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重组蛋白的3篇参考文献示例，涵盖表达、结构及功能研究：
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1. **文献名称**：*"Heterologous Expression and Functional Analysis of Human Fatty Acid Synthase in Saccharomyces cerevisiae"*
**作者**：Zhang Y. et al.
**摘要**：本研究利用酵母系统成功表达重组人脂肪酸合酶(FAS)，并验证其催化脂肪酸合成的活性，为代谢疾病研究提供工具。
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2. **文献名称**：*"Crystal Structure of the FAS Death Domain Complex Reveals Mechanistic Insights into Apoptotic Signaling"*
**作者**：Lee C. et al.
**摘要**：通过重组表达FAS受体死亡结构域蛋白，解析其与FADD蛋白的复合物晶体结构，揭示FAS介导凋亡信号的关键相互作用。
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3. **文献名称**：*"Recombinant Soluble FAS Ligand Inhibits Tumor Growth via Induction of Apoptosis in Vivo"*
**作者**：Johnson R. et al.
**摘要**：开发可溶性重组FAS配体蛋白，证明其通过激活凋亡通路显著抑制小鼠模型中肿瘤生长，提示其治疗潜力。
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4. **文献名称**：*"Engineering Recombinant FASN Truncated Proteins for Targeted Lipid Biosynthesis Studies"*
**作者**：Smith J. et al.
**摘要**：构建并纯化FASN截短重组蛋白，用于解析不同结构域在脂质合成中的功能，为开发特异性抑制剂奠定基础。
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注：以上文献为示例性内容，实际研究中可根据具体需求在PubMed或Google Scholar检索真实文献。
Fatty Acid Synthase (FAS) is a multifunctional enzyme complex central to *de novo* lipogenesis, catalyzing the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA. In mammals, FAS exists as a homodimeric protein, with each monomer containing seven distinct catalytic domains that orchestrate substrate shuttling through a series of condensation, reduction, and dehydration reactions. This enzyme plays a pivotal role in energy storage, membrane synthesis, and cellular signaling, with dysregulation linked to metabolic disorders, obesity, and cancer.
The recombinant production of FAS proteins has become a critical tool for studying its structure-function relationships and regulatory mechanisms. Traditional purification of native FAS from tissues is challenging due to low abundance and structural complexity. Recombinant DNA technology enables high-yield expression in systems like *E. coli*, insect cells, or mammalian cells, often with affinity tags for simplified purification. However, achieving proper folding and maintaining the stability of this large (~270 kDa per monomer) multidomain protein remains technically demanding.
Recombinant FAS is widely used to investigate enzymatic kinetics, allosteric regulation, and inhibitor screening for therapeutic development. Its overexpression in certain cancers has spurred interest in FAS-targeted anticancer agents. Structural studies using recombinant FAS, including cryo-EM and X-ray crystallography, have revealed dynamic conformational changes during catalysis. Additionally, engineered FAS variants facilitate exploration of substrate specificity and evolutionary adaptations across species. Beyond biomedical research, recombinant FAS serves as a biocatalyst for sustainable production of fatty acid derivatives in synthetic biology. Continued optimization of expression systems and purification protocols aims to enhance accessibility of this multifunctional enzyme for both basic and applied research.
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