Anti-human CD36

Monoclonal antibody FA6-152 recognizes human CD36 (88-kDa), a cell surface class B scavenger receptor, also known as thrombospondin receptor CD36 is a heavily N-glycosylated transmembrane protein of ~88 kDa with two short intracellular domains and a large extracellular domain. The protein is sensitive for neuroaminidase, resulting in a shift from 88 to 85 kDa. CD36 is expressed on platelets, mature monocytes and macrophages, microvascular endothelial cells, mammary endothelial cells, during stages of erythroid cell development and on some macrophage derived dendritic cells. The antibody recognizes adult and fetal monocytes, platelets and reticulocytes, but doesn't stain lymphocytes and granulocytes. Reactivity has also been found in small intestine, kidney, liver and thyroid. CD36 expression is primarily controlled by the transcription heterodimer PPARg-RXR (peroxisome proliferator-activated receptor-g-retinoid-X-receptor). CD36 is preferentially found within lipid rafts, which facilitates its association with receptors, signaling and adaptor molecules. It is a receptor and transporter of oxidized lipids and long chain fatty acids. CD36 has been implicated in many biological processes including angiogenesis, phagocytosis, inflammation, and lipid and glucose metabolism. Several in vivo models support the role of the thrombospondin / CD36 system in angiogenesis and tumor growth. An important role for CD36 has been found in Malaria as major receptor for P. falciparum-infected red blood cells. CD36 is associated with Src-family kinases and with the integrins alpha3 beta1 and alpha6 beta1. Recently, CD36 has been identified as a protein that is required for toll like receptor (TLR2) recognition of di-acylated bacterial lipopeptides and lipoteichoic acid4. Furthermore, CD36 has been shown to function as phagocytic receptor for apoptotic cells. Many different ligands have been reported to interact with CD36, suggesting that CD36 could recognize a structure-based domain rather than specific contact residues. Monoclonal antibody FA6-152 blocks the biological activity of CD36 by blocking collagen/thrombospondin binding. The antibody agglutinates fetal but not adult erythrocytes. Protein function: Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (PubMed:18353783, PubMed:21610069). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (PubMed:18753675). Involved in oral fat perception and preferences (PubMed:22240721, PubMed:25822988). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions. In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract. Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis. Receptor for thombospondins, THBS1 and THBS2, mediating their antiangiogenic effects. As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome (PubMed:20037584). Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). [The UniProt Consortium]