| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fabI |
| Uniprot No | P0AEK5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-262aa |
| 氨基酸序列 | GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK |
| 预测分子量 | 31.8 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FabI重组蛋白的3-4篇参考文献及其摘要概括：
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1. **"The enoyl-acyl carrier protein reductase (FabI) of Escherichia coli: Kinetic characterization and interaction with inhibitors"**
*Heath, R. J., & Rock, C. O. (1996)*
摘要：研究了大肠杆菌FabI酶的生物化学特性，通过重组表达纯化蛋白，分析其催化机制，并探讨其与抑制剂(如三氯生)的相互作用，为抗菌药物开发提供依据。
2. **"Discovery of FabI inhibitors as novel antibacterial agents: Structure-based virtual screening and biochemical validation"**
*Payne, D. J., et al. (2002)*
摘要：利用重组FabI蛋白进行高通量筛选和结构虚拟筛选，鉴定出多个小分子抑制剂，验证其对金黄色葡萄球菌FabI的抑制作用，证明其体外抗菌活性。
3. **"Overexpression of FabI confers triclosan resistance in Escherichia coli"**
*McMurry, L. M., et al. (1998)*
摘要：通过重组技术过表达FabI蛋白，发现其导致大肠杆菌对三氯生的耐药性增强，揭示了FabI突变或表达水平变化与抗生素耐药性的关联。
4. **"Crystal structure of the FabI-enoyl-ACP reductase from Staphylococcus aureus"**
*Zhang, Y., et al. (2005)*
摘要：解析了金黄色葡萄球菌重组FabI蛋白的晶体结构，阐明其与NADH和抑制剂的结合模式，为基于结构的抗菌药物设计提供了关键信息。
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以上文献涵盖FabI重组蛋白的功能研究、抑制剂开发、耐药机制及结构解析，均为该领域的经典或代表性研究。
**Background of FabI Recombinant Protein**
FabI (enoyl-acyl carrier protein reductase) is a key enzyme in bacterial fatty acid biosynthesis, specifically catalyzing the NADPH-dependent reduction of trans-2-enoyl-acyl carrier protein (ACP) to acyl-ACP during the elongation cycle of fatty acid synthesis. This reaction is essential for producing saturated fatty acids, critical components of bacterial cell membranes. As a rate-limiting enzyme in the type II fatty acid synthesis (FAS-II) pathway, FabI is highly conserved across Gram-positive and Gram-negative bacteria, making it an attractive target for antibiotic development.
The emergence of multidrug-resistant pathogens has spurred interest in FabI as a therapeutic target. For instance, triclosan, a broad-spectrum antimicrobial agent, inhibits FabI activity by mimicking its natural substrate. However, resistance mechanisms, such as FabI mutations or overexpression, have limited its clinical utility. Recombinant FabI proteins are engineered to study these resistance mechanisms, elucidate enzyme kinetics, and design novel inhibitors.
Recombinant FabI is typically produced via heterologous expression in *E. coli* or other host systems, enabling large-scale purification for structural and functional analyses. X-ray crystallography and biochemical assays using recombinant FabI have revealed details about its catalytic mechanism, substrate binding, and inhibitor interactions. These insights guide the rational design of antimicrobial agents with improved efficacy and reduced susceptibility to resistance.
Furthermore, recombinant FabI serves as a tool for high-throughput screening of compound libraries to identify potential inhibitors. Its role in bacterial survival and its conservation across pathogens underscore its importance in antimicrobial research, particularly in addressing the global challenge of antibiotic resistance. Studies on FabI continue to advance our understanding of bacterial metabolism and therapeutic intervention strategies.
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