| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fabG |
| Uniprot No | P0AEK2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-244aa |
| 氨基酸序列 | MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV |
| 预测分子量 | 33.0 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fabG重组蛋白的3篇示例参考文献(信息为示例，具体文献需通过学术数据库验证)：
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1. **标题**：*Cloning, expression, and characterization of the fabG gene from Escherichia coli*
**作者**：Zhang Y, Cronan JE
**摘要**：研究报道了大肠杆菌fabG基因的克隆及重组蛋白在大肠杆菌中的高效表达与纯化，分析了FabG的酶动力学特性，证实其在脂肪酸合成中的关键还原酶功能。
2. **标题**：*Structural insights into the catalytic mechanism of FabG in bacterial fatty acid biosynthesis*
**作者**：Leesong M, et al.
**摘要**：通过X射线晶体学解析FabG蛋白的三维结构，揭示了其NADPH结合位点及底物相互作用机制，为设计新型抗菌药物提供结构基础。
3. **标题**：*Metabolic engineering of FabG for enhanced biofuel production in Saccharomyces cerevisiae*
**作者**：Li H, Liao JC
**摘要**：研究通过重组表达优化FabG酶活性，改造酵母代谢途径以提高中链脂肪酸产量，为生物燃料生产提供新策略。
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如需准确引用，建议通过PubMed、Web of Science或Google Scholar检索关键词“fabG recombinant protein”或结合具体研究方向筛选文献。
**Background of FabG Recombinant Protein**
FabG, encoded by the *fabG* gene, is a critical enzyme in bacterial fatty acid biosynthesis. It belongs to the type II fatty acid synthesis (FAS II) pathway, a system distinct from the mammalian FAS I pathway, making it an attractive target for antimicrobial drug development. FabG functions as a β-ketoacyl-ACP reductase, catalyzing the NADPH-dependent reduction of β-ketoacyl-acyl carrier protein (ACP) intermediates to β-hydroxyacyl-ACP during fatty acid elongation. This step is essential for maintaining the structural integrity of bacterial cell membranes and energy storage.
Recombinant FabG protein is produced via heterologous expression in bacterial hosts (e.g., *E. coli*), enabling large-scale purification for functional and structural studies. Its recombinant form retains enzymatic activity, facilitating investigations into substrate specificity, inhibitor screening, and mechanistic insights. Researchers often employ affinity tags (e.g., His-tag) to streamline purification, followed by biochemical assays to validate activity.
FabG’s role in bacterial survival, coupled with its absence in humans, underscores its potential as a target for novel antibiotics. Inhibitors disrupting FabG activity could selectively impair pathogenic bacteria without harming host cells. Additionally, FabG variants have been engineered for metabolic engineering applications, such as synthesizing biofuels or specialized lipids.
Structural studies of recombinant FabG (via X-ray crystallography or cryo-EM) reveal conserved catalytic domains and cofactor-binding sites, aiding rational drug design. Mutational analyses highlight residues critical for NADPH binding and substrate interaction, informing enzyme engineering efforts.
Overall, FabG recombinant protein serves as a vital tool for understanding bacterial lipid metabolism, advancing antimicrobial discovery, and enabling biotechnological applications. Its study bridges fundamental biochemistry and translational research, addressing challenges in antibiotic resistance and sustainable bio-production.
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