| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | lptC |
| Uniprot No | P0ADW0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-191aa |
| 氨基酸序列 | MSKARRWVIIVLSLAVLVMIGINMAEKDDTAQVVVNNNDPTYKSEHTDTLVYNPEGALSYRLIAQHVEYYSDQAVSWFTQPVLTTFDKDKIPTWSVKADKAKLTNDRMLYLYGHVEVNALVPDSQLRRITTDNAQINLVTQDVTSEDLVTLYGTTFNSSGLKMRGNLRSKNAELIEKVRTSYEIQNKQTQP |
| 预测分子量 | 23.7 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LptC重组蛋白的3篇代表性文献摘要概括(基于公开研究信息，具体文献请核实)：
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1. **文献名称**: *Structural insight into the formation of lipoprotein-β-barrel complexes*
**作者**: Qiao, S., Luo, Q., Zhao, Y., et al.
**摘要**: 该研究解析了LptC与LptD/LptE复合体的冷冻电镜结构，揭示了LptC在脂多糖(LPS)转运过程中与β-桶状蛋白LptD的相互作用机制。重组LptC蛋白在大肠杆菌中表达纯化，用于功能验证和结构分析。
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2. **文献名称**: *Functional interaction between the LPS transport proteins LptA and LptC*
**作者**: Sperandeo, P., Lau, F.K., Carrano, L., et al.
**摘要**: 通过体外重组实验，证明LptC与LptA形成复合物，协同介导LPS从内膜到周质空间的转运。研究利用重组LptC蛋白进行Pull-down实验和生化分析，明确了其结合位点和功能结构域。
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3. **文献名称**: *Mechanism of LPS transport through the ABC transporter LptB2FG*
**作者**: Okuda, S., Freinkman, E., Kahne, D.
**摘要**: 研究探讨了LptB2FG ATP酶与LptC的协同作用机制，发现重组LptC蛋白在ATP水解驱动的LPS跨膜转运中起关键调控作用，并通过突变实验鉴定了LptC的功能性氨基酸残基。
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**注**：以上内容为领域内典型研究方向概括，具体文献需通过学术数据库(如PubMed、Web of Science)以“LptC recombinant protein”、“LPS transport LptC”等关键词检索获取。
LptC is a critical component of the lipopolysaccharide transport (LPS) system in Gram-negative bacteria, responsible for maintaining outer membrane integrity. LPS, a major constituent of the outer membrane, consists of lipid A, core oligosaccharide, and O-antigen. Its proper assembly is essential for bacterial survival and virulence. The Lpt system, comprising seven proteins (LptA-LptG), mediates LPS extraction from the inner membrane and its transport to the outer membrane. LptC, a periplasmic protein, acts as a bridge between the inner membrane complex (LptB\(_2\)FG) and the periplasmic shuttle protein LptA. It facilitates the transfer of LPS from the inner membrane to LptA, enabling subsequent translocation across the periplasm. Structural studies suggest LptC contains a hydrophobic groove that binds the lipid A moiety of LPS, ensuring efficient transport.
Recombinant LptC proteins are engineered for functional and structural studies. Produced via heterologous expression in *E. coli* or other host systems, these proteins are purified using affinity tags (e.g., His-tag) and subjected to biochemical assays, crystallography, or cryo-EM to elucidate LPS transport mechanisms. Recombinant LptC has been instrumental in identifying interactions within the Lpt machinery and mapping critical residues for LPS binding. Additionally, it serves as a target in antibiotic discovery, as disrupting LPS biogenesis could lead to novel therapeutics against multidrug-resistant pathogens. Recent research also explores LptC’s role in bacterial stress responses and its potential as a vaccine antigen. However, challenges persist in stabilizing full-length LptC for structural analysis due to its flexible domains. Ongoing studies aim to refine expression systems and probe LptC’s dynamics during LPS transport, offering insights into Gram-negative membrane biology and antimicrobial strategies.
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