| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fadL |
| Uniprot No | Q8XCN6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-446aa |
| 氨基酸序列 | AGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGKTPQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRVFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAYTSWSQFQQLKATSTSGDTLFQKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF |
| 预测分子量 | 61.9 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. |
1. **"Structural basis for long-chain fatty acid transport by the outer membrane protein FadL"**
- **作者**: Black, P.N., et al.
- **摘要**: 研究解析了大肠杆菌FadL蛋白的晶体结构，揭示了其独特的β-桶状跨膜结构域和内部底物通道，阐明了长链脂肪酸选择性转运的分子机制。
2. **"Expression and purification of recombinant FadL protein from Escherichia coli: Functional analysis of fatty acid transport"**
- **作者**: Kumar, R., et al.
- **摘要**: 报道了通过大肠杆菌重组表达系统高效表达FadL蛋白的方法，并验证纯化后蛋白在体外模型中结合和转运脂肪酸的活性。
3. **"Mechanistic insights into FadL-mediated fatty acid uptake across the bacterial outer membrane"**
- **作者**: Ma, Y., et al.
- **摘要**: 通过X射线晶体学和突变实验，揭示了FadL蛋白N端延伸区域的动态构象变化在脂肪酸跨外膜转运中的关键作用。
4. **"Functional characterization of FadL homologs in Gram-negative bacteria: Role in nutrient transport"**
- **作者**: Nikaido, H.
- **摘要**: 综述了FadL及其同源蛋白在革兰氏阴性菌中的保守性，探讨其作为疏水性小分子转运通道的通用机制及生理意义。
(注：以上文献信息为示例，实际引用需根据具体论文调整。)
FadL is an outer membrane protein in *Escherichia coli* responsible for the uptake of long-chain fatty acids, essential for bacterial metabolism and energy production. It belongs to the FadL family of transporters, which facilitate the diffusion of hydrophobic molecules across the outer membrane. Structurally, FadL features a characteristic β-barrel domain embedded in the membrane and a unique N-terminal "hat" domain that controls substrate entry. Its function is critical for fatty acid degradation (fad) pathways, enabling bacteria to utilize external fatty acids as carbon sources.
Recombinant FadL protein refers to the engineered version produced via heterologous expression systems, such as *E. coli* or yeast, for biochemical and structural studies. The cloning and overexpression of the *fadL* gene allow large-scale purification, enabling researchers to investigate its transport mechanism, substrate specificity, and interaction with other cellular components. X-ray crystallography and cryo-EM studies using recombinant FadL have revealed conformational changes during fatty acid binding and translocation, highlighting its role in substrate gating and membrane dynamics.
Interest in recombinant FadL also stems from its potential biotechnological applications. Its ability to transport hydrophobic molecules has inspired efforts to engineer it for biofuel production or drug delivery systems. Additionally, studying FadL aids in understanding antibiotic resistance mechanisms, as outer membrane proteins in pathogenic bacteria often share structural similarities. Challenges in recombinant production include maintaining proper folding and solubility, often addressed through fusion tags or optimized expression conditions. Overall, FadL serves as a model system for membrane protein research and a tool for synthetic biology innovations.
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