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CLEC5A encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Zusätzlich bieten wir Ihnen CLEC5A Antikörper (65) und CLEC5A Proteine (10) und viele weitere Produktgruppen zu diesem Protein an.
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CLEC5A is critical for dengue virus-induced osteoclast activation and bone homeostasis
Mannose Receptor and CLEC5A on Macrophage first attracts the Dengue Virus with high avidity, and the virus concurrently interacts with CLEC5A in close proximity to form a multivalent hetero-complex and facilitate CLEC5A-mediated signal transduction. Dengue Virus Infection Is through a Cooperative Interaction between a Mannose Receptor and CLEC5A on Macrophage as a Multivalent Hetero-Complex.
The results suggest that CLEC5A-mediated enhancement of the inflammatory response in myeloid cells contributes to influenza pathogenicity in vivo and may be considered a therapeutic target in combination with effective antivirals.
Concordant overexpression of MDL-1 and DAP12 (zeige TYROBP ELISA Kits) were correlated with increased production of proinflammatory cytokines in rheumatoid arthritis patients.
Blockade of CLEC5A inhibits NLRP3 (zeige NLRP3 ELISA Kits) inflammasome activation and pyrotopsis in dengue-virus-infected inflammatory macrophages. Thus, DV can activate NLRP3 (zeige NLRP3 ELISA Kits) 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 (zeige TPM2 ELISA Kits), 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)
Data show that C-type lectin member 5A (CLEC5A) is needed for optimal reactive oxygen species (ROS (zeige ROS1 ELISA Kits)) production, neutrophil extracellular traps (NETs) formation and other immune responses to Listeria monocytogenes in mice.
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 (zeige TYROBP ELISA Kits) phosphorylation in macrophages.
triggering of MDL-1 on immature myeloid cells and production of NO and TNF-alpha (zeige TNF ELISA Kits) 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 (zeige TYROBP ELISA Kits) and DAP10 (zeige HCST ELISA Kits) in osteoclasts and bone marrow-derived macrophages, where DAP10 (zeige HCST ELISA Kits) association depends almost entirely on DAP12 (zeige TYROBP ELISA Kits), suggesting a formation of MDL-1-DAP12 (zeige TYROBP ELISA Kits)/DAP10 (zeige HCST ELISA Kits) 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