纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | fabD |
Uniprot No | Q5HGK3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-308aa |
氨基酸序列 | MSKTAIIFPGQGAQKVGMAQDLFNNNDQATEILTSAANTLDFDILETMFTDEEGKLGETENTQPALLTHSSALLAALKNLNPDFTMGHSLGEYSSLVAADVLSFEDAVKIVRKRGQLMAQAFPTGVGSMAAVLGLDFDKVDEICKSLSSDDKIIEPANINCPGQIVVSGHKALIDELVEKGKSLGAKRVMPLAVSGPFHSSLMKVIEEDFSSYINQFEWRDAKFPVVQNVNAQGETDKEVIKSNMVKQLYSPVQFINSTEWLIDQGVDHFIEIGPGKVLSGLIKKINRDVKLTSIQTLEDVKGWNEND |
预测分子量 | 35.6 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 **fabD重组蛋白** 的3篇示例文献(注:内容为示例,非真实文献):
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1. **文献名称**:*Structural and functional characterization of FabD from Staphylococcus aureus*
**作者**:Smith A, et al.
**摘要**:解析金黄色葡萄球菌FabD蛋白的晶体结构,阐明其催化丙二酰-CoA向酰基载体蛋白(ACP)转移的分子机制,为开发靶向脂肪酸合成的抗菌药物提供结构基础。
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2. **文献名称**:*Heterologous expression and purification of recombinant FabD in E. coli for enzymatic assays*
**作者**:Lee B, et al.
**摘要**:报道在大肠杆菌中高效表达和纯化重组FabD蛋白的方法,优化表达条件及纯化步骤,验证其体外酶活性和稳定性,为脂肪酸合成途径研究提供工具蛋白。
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3. **文献名称**:*Role of FabD in bacterial fatty acid biosynthesis and antibiotic resistance*
**作者**:Zhang C, et al.
**摘要**:探讨FabD在细菌脂肪酸合成中的关键作用,通过基因敲除实验证明其与细菌生长及β-内酰胺类抗生素耐药性的关联,提示FabD作为潜在抗菌靶点的价值。
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(注:以上文献信息为示例性内容,实际文献需通过学术数据库检索确认。)
**Background of FabD Recombinant Protein**
FabD, encoded by the *fabD* gene, is a key enzyme in bacterial fatty acid biosynthesis. It catalyzes the transacylation of malonyl group from malonyl-CoA to the acyl carrier protein (ACP), forming malonyl-ACP, an essential substrate for fatty acid elongation. This reaction is a critical step in the type II fatty acid synthesis (FAS II) pathway, which is distinct from the mammalian FAS I system and thus represents a potential target for antibacterial drug development.
FabD’s role in bacterial survival and its absence in humans make it an attractive candidate for studying novel antimicrobial agents, particularly against drug-resistant pathogens. Recombinant FabD protein is produced via heterologous expression systems (e.g., *E. coli*) using genetic engineering techniques. Cloning the *fabD* gene into expression vectors allows large-scale production of the purified enzyme for structural, functional, and inhibitory studies.
Research on recombinant FabD has provided insights into its catalytic mechanism, substrate specificity, and interactions with inhibitors. Structural studies, including X-ray crystallography, have revealed its dimeric architecture and active-site residues critical for substrate binding. Additionally, FabD’s conservation across Gram-positive and Gram-negative bacteria underscores its broad relevance in microbial physiology and as a therapeutic target.
Beyond antimicrobial applications, FabD recombinant protein is utilized in synthetic biology and metabolic engineering to modify fatty acid pathways for biofuel or specialty chemical production. Its study also contributes to understanding bacterial resistance mechanisms, such as mutations affecting enzyme-inhibitor interactions. Overall, FabD recombinant protein serves as a vital tool for both basic research and biotechnological innovation.
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