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CLEC5A encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Additionally we are shipping CLEC5A Antibodies (50) and CLEC5A Kits (3) and many more products for this protein.
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Concordant overexpression of MDL-1 and DAP12 (show TYROBP Proteins) were correlated with increased production of proinflammatory cytokines in rheumatoid arthritis patients.
Blockade of CLEC5A inhibits NLRP3 (show NLRP3 Proteins) inflammasome activation and pyrotopsis in dengue-virus-infected inflammatory macrophages. Thus, DV can activate NLRP3 (show NLRP3 Proteins) inflammasome via CLEC5A.
No significant associations were noted between the genotypes and allele frequency of the 4 CLEC5A tSNPs between controls and Kawasaki disease patients.
CLEC5A is homodimeric at the cell surface and binds to dengue virus serotypes 1-4.
CLEC5A expression in monocyte/macrophage and granulocytes is regulated by PU.1.
The crystal volume per unit weight (VM) was calculated to be 2.34 A3 Da-1 (show TPM2 Proteins), with nine molecules per asymmetric unit and a solvent content of 47.38%. CLEC5A plays an important role in the pathophysiology of dengue-virus-induced disease.
blockade of CLEC5A-mediated signalling attenuates the production of proinflammatory cytokines by macrophages infected with Dengue virus (either alone or complexed with an enhancing antibody)
cigarette smoke-induced macrophage responsiveness is mediated by CLEC5A, and CLEC5A is required for the development of inflammation, proinflammatory cytokine expression, and airspace enlargement.
Japanese encephalitis virus (JEV) directly interacts with CLEC5A and induces DAP12 (show TYROBP Proteins) phosphorylation in macrophages.
triggering of MDL-1 on immature myeloid cells and production of NO and TNF-alpha (show TNF Proteins) may play a critical role in the pathogenesis of shock
This is the first report that shows the involvement of monocyte and macrophage receptor CLEC5A in severe inflammatory response in Japanese encephalitis virus (JEV) infection of brain.
Activation of MDL-1 leads to enhanced recruitment of inflammatory macrophages and neutrophils to the joint and promotes bone erosion.
MDL-1 plays an important role in immune defense as a result of an innate immunity, which involves neutrophils and macrophages
MDL-1 associates with both DAP12 (show TYROBP Proteins) and DAP10 (show HCST Proteins) in osteoclasts and bone marrow-derived macrophages, where DAP10 (show HCST Proteins) association depends almost entirely on DAP12 (show TYROBP Proteins), suggesting a formation of MDL-1-DAP12 (show TYROBP Proteins)/DAP10 (show HCST Proteins) trimolecular complexes.
This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type II transmembrane protein interacts with dnax-activation protein 12 and may play a role in cell activation. Alternative splice variants have been described but their full-length sequence has not been determined.
C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 5
, C-type lectin domain family 5 member A
, C-type lectin superfamily member 5
, myeloid DAP12-associating lectin 1
, myeloid DAP12-associating lectin-1
, myeloid DAP12-associating lectin long form
, type II transmembrane protein MDL-1