| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | lolA |
| Uniprot No | A7ZYJ5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-203aa |
| 氨基酸序列 | DAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKSQQNGAVDAAKFTFTPPQGVTVDDQRK |
| 预测分子量 | 22.3 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lolA重组蛋白的3篇代表性文献及其摘要简述(基于公开领域知识模拟，非真实文献)：
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1. **文献名称**: *Cloning, expression, and characterization of the lolA gene encoding a lipoprotein transporter in Escherichia coli*
**作者**: Tanaka et al.
**摘要**: 该研究首次克隆并表达了大肠杆菌中的lolA基因，验证其编码的蛋白在细菌脂蛋白转运中的关键作用。通过重组蛋白体外实验，证明LolA能与脂蛋白前体结合，并依赖ATP将其转运至外膜。
2. **文献名称**: *Structural insights into LolA-mediated lipoprotein trafficking in Gram-negative bacteria*
**作者**: Matsuyama et al.
**摘要**: 利用X射线晶体学解析了重组LolA蛋白的三维结构，揭示了其疏水腔结合脂蛋白的分子机制，并阐明了LolA与伴侣蛋白LolB的相互作用模式，为抗菌药物靶点设计提供结构基础。
3. **文献名称**: *Development of a recombinant LolA-based vaccine against Pseudomonas aeruginosa infections*
**作者**: Zhang et al.
**摘要**: 研究通过重组表达铜绿假单胞菌LolA蛋白，评估其作为疫苗抗原的潜力。动物实验表明，重组LolA可诱导特异性抗体，显著提高小鼠对细菌感染的存活率，提示其在抗感染免疫中的应用前景。
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注：以上内容为领域知识模拟，实际文献需通过学术数据库(如PubMed、Web of Science)检索。
**Background of lolA Recombinant Protein**
The lolA protein is a key component of the lipoprotein transport system in Gram-negative bacteria, primarily involved in the localization of lipoproteins to the outer membrane. Lipoproteins play critical roles in bacterial physiology, including nutrient uptake, cell envelope integrity, and virulence. The lol (lipoprotein localization) system, comprising LolABCDE proteins, facilitates the ATP-dependent transfer of lipoproteins from the inner membrane to the outer membrane. Among these, LolA acts as a chaperone, binding to lipoproteins released by the LolCDE complex and shuttling them through the periplasm to LolB, which mediates their insertion into the outer membrane.
Recombinant lolA is produced via genetic engineering, typically by cloning the *lolA* gene into expression vectors (e.g., *E. coli*), followed by purification using affinity chromatography. Its soluble, stable nature makes it amenable to structural and functional studies. Structurally, lolA forms a β-barrel structure with a hydrophobic cavity for lipoprotein binding, a feature critical for its chaperone function.
Research on lolA has focused on its role in bacterial pathogenesis and potential as a therapeutic target. Inhibiting lolA disrupts lipoprotein trafficking, compromising bacterial viability and virulence, making it attractive for antibiotic development. Additionally, lolA recombinant protein is used to study protein-protein interactions, lipid binding mechanisms, and structural dynamics via techniques like X-ray crystallography and cryo-EM. Its applications extend to vaccine development, as surface-exposed lipoproteins are often immunogenic.
Overall, lolA recombinant protein serves as a vital tool for understanding bacterial lipoprotein trafficking and developing novel antimicrobial strategies.
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