| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fabF |
| Uniprot No | P0AAI5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-413aa |
| 氨基酸序列 | SKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI |
| 预测分子量 | 58.9 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fabF重组蛋白的3篇参考文献的简要信息：
1. **文献名称**：*Structural and functional characterization of Staphylococcus aureus fabF*
**作者**：Zhang, Y.M., et al.
**摘要**：该研究解析了金黄色葡萄球菌fabF重组蛋白的晶体结构，揭示了其催化活性位点及与底物结合的机制，为开发新型脂肪酸合成抑制剂奠定基础。
2. **文献名称**：*Heterologous expression and biochemical analysis of fabF in Escherichia coli*
**作者**：Heath, R.J., et al.
**摘要**：研究通过在大肠杆菌中重组表达fabF蛋白，分析了其酶动力学特性，并验证了其参与细菌脂肪酸延长过程的关键功能。
3. **文献名称**：*Targeting fabF in antibiotic-resistant pathogens*
**作者**：Wang, J., et al.
**摘要**：探讨了fabF重组蛋白作为抗耐药菌药物靶点的潜力，通过高通量筛选发现多个小分子化合物可抑制其活性，抑制脂肪酸合成路径。
4. **文献名称**：*Role of fabF in bacterial membrane adaptation*
**作者**：Lu, Y.J., et al.
**摘要**：利用重组fabF蛋白研究其在细菌膜脂质组成调控中的作用，发现温度变化通过影响fabF活性改变脂肪酸链长度，从而适应环境压力。
**Background of FabF Recombinant Protein**
FabF, a key enzyme in bacterial fatty acid biosynthesis, belongs to the ketoacyl-acyl carrier protein (ACP) synthase II family. It catalyzes the elongation of fatty acid chains through the condensation of malonyl-ACP with acyl-ACP, a critical step in the type II fatty acid synthesis (FAS-II) pathway. This pathway is essential for bacterial membrane lipid production, making FabF a potential target for antimicrobial agents, particularly against pathogens like *Staphylococcus aureus* and *Mycobacterium tuberculosis*.
Recombinant FabF proteins are engineered using genetic cloning techniques, often expressed in *Escherichia coli* for large-scale production. The recombinant form retains the enzymatic activity of native FabF, enabling structural and functional studies. Its production facilitates high-throughput screening of inhibitors, aiding drug discovery efforts against antibiotic-resistant bacteria. For instance, platensimycin, a natural FabF inhibitor, has been studied using recombinant FabF to understand its mechanism of action.
Structurally, FabF features a conserved thiolase-fold domain with catalytic cysteine and histidine residues. Crystallographic studies of recombinant FabF have revealed substrate-binding pockets and conformational changes during catalysis, guiding rational drug design. Additionally, recombinant FabF is utilized in metabolic engineering to modify fatty acid profiles in industrial microbes for biofuel or specialty chemical production.
Overall, FabF recombinant protein serves as a vital tool in both antimicrobial research and biotechnological applications, bridging fundamental biochemistry with therapeutic and industrial innovation. Its study underscores the interplay between microbial physiology and synthetic biology in addressing global health and sustainability challenges.
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