| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | lptD |
| Uniprot No | P31554 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-784aa |
| 氨基酸序列 | ADLASQ CMLGVPSYDR PLVQGDTNDL PVTINADHAK GDYPDDAVFT GSVDIMQGNS RLQADEVQLH QKEAPGQPEP VRTVDALGNV HYDDNQVILK GPKGWANLNT KDTNVWEGDY QMVGRQGRGK ADLMKQRGEN RYTILDNGSF TSCLPGSDTW SVVGSEIIHD REEQVAEIWN ARFKVGPVPI FYSPYLQLPV GDKRRSGFLI PNAKYTTTNY FEFYLPYYWN IAPNMDATIT PHYMHRRGNI MWENEFRYLS QAGAGLMELD YLPSDKVYED EHPNDDSSRR WLFYWNHSGV MDQVWRFNVD YTKVSDPSYF NDFDNKYGSS TDGYATQKFS VGYAVQNFNA TVSTKQFQVF SEQNTSSYSA EPQLDVNYYQ NDVGPFDTRI YGQAVHFVNT RDDMPEATRV HLEPTINLPL SNNWGSINTE AKLLATHYQQ TNLDWYNSRN TTKLDESVNR VMPQFKVDGK MVFERDMEML APGYTQTLEP RAQYLYVPYR DQSDIYNYDS SLLQSDYSGL FRDRTYGGLD RIASANQVTT GVTSRIYDDA AVERFNISVG QIYYFTESRT GDDNITWEND DKTGSLVWAG DTYWRISERW GLRGGIQYDT RLDNVATSNS SIEYRRDEDR LVQLNYRYAS PEYIQATLPK YYSTAEQYKN GISQVGAVAS WPIADRWSIV GAYYYDTNAN KQADSMLGVQ YSSCCYAIRV GYERKLNGWD NDKQHAVYDN AIGFNIELRG LSSNYGLGTQ EMLRSNILPY QNTL |
| 预测分子量 | 89,6 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. |
1. **Title**: "Structural basis of outer membrane protein insertion by the BAM complex"
**Authors**: Dong, H., et al.
**Summary**: 解析了LptD与BAM复合物协同组装机制，利用重组蛋白技术阐明LptD在细菌外膜整合过程中的构象变化及其对脂多糖转运的关键作用。
2. **Title**: "LptD forms a membrane ring-like structure crucial for LPS transport"
**Authors**: Qiao, S., et al.
**Summary**: 通过重组LptD蛋白的冷冻电镜分析，揭示其形成β-桶状结构并与LptE互作，直接参与脂多糖(LPS)从周质到外膜表面的跨膜运输。
3. **Title**: "Antibiotic targeting of the LPS transporter complex LptD/E"
**Authors**: Srinivas, N., et al.
**Summary**: 研究基于重组LptD/E复合体筛选小分子抑制剂，发现新型抗生素通过破坏LptD-E相互作用阻断LPS运输，为革兰氏阴性菌耐药性问题提供新策略。
4. **Title**: "Reconstitution of the LptD-dependent LPS assembly pathway in vitro"
**Authors**: Chng, S.S., et al.
**Summary**: 利用重组LptD蛋白建立体外重建模型，验证其在LPS插入外膜过程中的ATP依赖性机制，并证明其功能需要伴侣蛋白LptE的辅助。
(注：以上文献标题及作者为虚拟示例，实际文献需通过PubMed或SciHub等平台检索确认。)
**Background of LptD Recombinant Protein**
LptD, a key component of the lipopolysaccharide (LPS) transport machinery in Gram-negative bacteria, plays a critical role in outer membrane biogenesis. It forms a β-barrel protein complex with LptE to mediate the final stages of LPS translocation from the inner membrane to the outer leaflet of the outer membrane. This process is essential for bacterial viability, as the outer membrane acts as a protective barrier against antibiotics and environmental stressors. Due to its conserved function and surface exposure, LptD has emerged as a promising target for novel antimicrobial therapies, particularly against multidrug-resistant pathogens like *Pseudomonas aeruginosa* and *Escherichia coli*.
Recombinant LptD production is challenging due to its structural complexity, hydrophobicity, and dependence on proper folding with LptE. Researchers often employ heterologous expression systems, such as *E. coli*, to produce LptD for functional and structural studies. However, overexpression frequently leads to inclusion body formation, necessitating optimized expression conditions, chaperone co-expression, or refolding strategies. Structural analyses, including X-ray crystallography and cryo-EM, have revealed conformational dynamics during LPS transport, guiding the design of inhibitors that disrupt LptD-LPS or LptD-LptE interactions.
Beyond drug development, LptD recombinant proteins are explored as vaccine candidates. Its surface localization and conservation across Gram-negative species make it a potential target for broad-spectrum vaccines. However, immunogenicity challenges, such as poor antigenicity or immune evasion mechanisms, require further engineering, such as epitope focusing or fusion with carrier proteins.
Overall, LptD recombinant protein research bridges fundamental microbiology and translational applications, offering avenues to combat antibiotic resistance through innovative therapeutic and preventive strategies.
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