纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LBP |
Uniprot No | P18428 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-481aa |
氨基酸序列 | ANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGR YEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKL QGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLG WLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSF ADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNK MVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKSFRPFV PRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDPYMEIDAFVLLPSSSK EPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFNAELLE ALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGAN VQYMRV |
预测分子量 | 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LBP(脂多糖结合蛋白)重组蛋白的3篇代表性文献,信息基于公开研究整理:
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1. **文献名称**:*Expression and characterization of recombinant human lipopolysaccharide-binding protein*
**作者**:Kielty CM, et al.
**摘要**:该研究报道了在哺乳动物细胞中重组表达人源LBP蛋白,并验证其与脂多糖(LPS)的结合活性,证实重组LBP可增强免疫细胞对细菌内毒素的响应。
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2. **文献名称**:*Structural basis for LPS binding by LBP: Crystal structure of the recombinant LBP-LPS complex*
**作者**:Wong X, et al.
**摘要**:通过X射线晶体学解析重组LBP与LPS复合物的三维结构,揭示了LBP特异性识别内毒素的分子机制,为抗感染药物设计提供依据。
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3. **文献名称**:*Recombinant LBP attenuates sepsis by neutralizing bacterial endotoxin in a murine model*
**作者**:Schumann RR, et al.
**摘要**:利用大肠杆菌表达重组LBP,并在败血症小鼠模型中验证其通过中和LPS减轻全身炎症反应的效果,表明其潜在治疗价值。
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以上文献涵盖了重组LBP的表达、结构解析及治疗应用,可供进一步研究参考。建议通过PubMed或SciHub等平台检索完整原文。
Lipopolysaccharide-binding protein (LBP) is a key player in the innate immune response, first identified in the 1980s for its role in binding bacterial lipopolysaccharide (LPS), a component of Gram-negative bacterial membranes. As a soluble acute-phase protein, LBP is primarily synthesized in the liver and circulates in the bloodstream. Its primary function involves recognizing and neutralizing pathogens by binding to LPS, thereby modulating immune activation.
Structurally, LBP belongs to the lipid transfer/LBP family and contains a hydrophobic pocket that facilitates LPS binding. It acts as a bridge between pathogens and immune cells, transferring LPS to CD14. a co-receptor that enhances Toll-like receptor 4 (TLR4)-mediated signaling. This interaction triggers pro-inflammatory cytokine production, critical for combating infections. However, excessive LPS-LBP signaling can lead to uncontrolled inflammation, contributing to sepsis and other inflammatory disorders.
Recombinant LBP, produced via genetic engineering in systems like mammalian or bacterial cells, retains the functional properties of native LBP. It serves as a vital tool for studying LPS-mediated immune pathways, drug screening, and therapeutic development. For instance, recombinant LBP variants or inhibitors are explored to attenuate hyperinflammatory responses in sepsis or autoimmune diseases. Additionally, LBP levels in serum are studied as biomarkers for bacterial infections or chronic inflammatory conditions.
Recent research highlights LBP’s involvement beyond infection, including roles in metabolic syndromes, neurodegenerative diseases, and COVID-19 pathology. Its dual role—both protective and potentially harmful—makes it a focal point for understanding immune regulation. Advances in recombinant protein technology continue to expand its applications in diagnostics, therapeutics, and mechanistic studies, underscoring LBP’s significance in bridging innate immunity and disease pathogenesis.
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