Recombinant Human LBP protein (His tag) is a Human Full Length protein, in the 1 to 481 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:24120359, PubMed:7517398). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:24120359, PubMed:7517398).
Lipopolysaccharide-binding protein, LBP
Recombinant Human LBP protein (His tag) is a Human Full Length protein, in the 1 to 481 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 8
Constituents: 0.58% Sodium chloride, 0.24% Tris, 0.001% EDTA
Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:24120359, PubMed:7517398). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:24120359, PubMed:7517398).
Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
Lipopolysaccharide-binding protein (LBP) also known as LPS-binding protein is an acute-phase protein that plays a critical role in the immune response to Gram-negative bacterial infections. This protein weighing approximately 60kDa is primarily expressed in the liver and found in the serum. LBP binds to lipopolysaccharides (LPS) which are components of the outer membrane of Gram-negative bacteria facilitating the transfer of LPS to CD14 receptors on immune cells. This transfer enhances the recognition of bacterial endotoxins triggering an immune response.
LBP serves a significant role in enhancing the sensitivity of the immune system to bacterial endotoxins. It does not form a permanent part of a larger complex but works closely with other molecules like CD14 and MD-2 an accessory protein of the TLR4 receptor to mediate the innate immune response. By efficiently binding LPS LBP aids in transporting these molecules to cell surface receptors accelerating the detection and subsequent response to infections.
LBP is heavily involved in the TLR4 signaling pathway which is important for the detection and response to Gram-negative bacterial infections. Through this pathway LBP and associated proteins such as CD14 and MD-2 help activate TLR4 triggering downstream NF-κB signaling. This activation leads to the production of pro-inflammatory cytokines and an upsurge in antimicrobial activities fortifying the body's defenses against bacterial invasion.
Enhanced LBP levels have been associated with sepsis a severe systemic response to bacterial infections which can often lead to septic shock. Given its pivotal role in recognizing bacterial endotoxins LBP is important in identifying infections making it a potential prospect for therapeutic targeting. Additionally its interaction with CD14 means that alterations in LBP function or expression levels might contribute to immune dysregulation seen in inflammatory diseases such as Crohn's disease where immune responses to gut microbiota play a central role.
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SDS-PAGE analysis of ab276289
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