| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LPS |
| Uniprot No | P43026 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 382-501aa |
| 氨基酸序列 | APLATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR |
| 预测分子量 | 13.6 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LPS(脂多糖)重组蛋白的3篇代表性文献，包含标题、作者及摘要概括：
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1. **标题**：*Recombinant LPS-binding protein (LBP) modulates inflammatory responses in sepsis models*
**作者**：Zhang Y, et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了重组LPS结合蛋白(LBP)，实验表明其能有效中和LPS诱导的炎症反应，在脓毒症小鼠模型中显著降低促炎因子(如TNF-α和IL-6)水平，提示其作为潜在抗炎治疗策略的可能性。
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2. **标题**：*Structural and functional characterization of recombinant lipid A biosynthetic enzymes in Gram-negative bacteria*
**作者**：Smith TJ, et al.
**摘要**：通过重组技术表达了革兰氏阴性菌中参与脂多糖(LPS)核心结构“脂质A”合成的关键酶(如LpxA和LpxD)，解析其晶体结构并验证其催化活性，为开发靶向LPS合成的抗菌药物提供理论依据。
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3. **标题**：*Recombinant outer membrane protein A (OmpA) as a vaccine adjuvant targeting TLR4 signaling*
**作者**：Lee S, et al.
**摘要**：研究利用重组表达的大肠杆菌外膜蛋白A(OmpA)，证明其通过TLR4受体激活免疫反应，显著增强小鼠对肺炎克雷伯菌的抗体应答，提示重组OmpA在疫苗佐剂开发中的应用潜力。
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**备注**：以上文献为示例，实际引用需根据具体研究领域调整。建议通过PubMed或Google Scholar以关键词“recombinant LPS protein”或“LPS-binding protein expression”检索最新文章。
Lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria, plays a critical role in bacterial pathogenicity and host immune responses. Structurally, LPS consists of three domains: the O-antigen polysaccharide, core oligosaccharide, and lipid A. Lipid A, the conserved hydrophobic moiety, is responsible for triggering innate immune responses via Toll-like receptor 4 (TLR4), often leading to septic shock in severe infections. Historically, native LPS extracted from bacteria has been used in research, but its structural heterogeneity and contamination risks prompted the development of recombinant LPS proteins.
Recombinant LPS proteins are engineered using genetic and biochemical techniques to isolate or modify specific components of LPS, particularly lipid A or O-antigen domains. This approach enables precise control over LPS structure, enhances reproducibility, and reduces endotoxin variability. For example, E. coli and other bacterial expression systems are employed to produce purified LPS subunits or fusion proteins. Such recombinant forms are invaluable in studying TLR4 signaling mechanisms, developing LPS-neutralizing therapies, and creating safer vaccine adjuvants. Lipid A analogs like monophosphoryl lipid A (MPL), produced recombinantly, retain immunostimulatory properties while minimizing toxicity, making them FDA-approved adjuvants in vaccines.
Challenges persist in replicating complex LPS glycosylation patterns and maintaining conformational stability. Nonetheless, recombinant LPS technology continues advancing immunotherapy, antimicrobial drug discovery, and our understanding of host-microbe interactions. Its applications extend to diagnostic tools, anti-endotoxin therapies, and synthetic biology for engineered bacterial membranes. By offering tailored molecular tools, recombinant LPS proteins bridge the gap between structural biology and translational medicine.
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