The FA6-152 antibody reacts with CD36, an ~88 kDa transmembrane glycoprotein that functions as a scavenger receptor, cell adhesion molecule, and signal transducer on the surface of many types of cells including platelets, monocytes, macrophages, erythrocyte precursors, endothelial and epithelial cells, and some macrophage-derived dendritic cells. The topology of the protein is thought to comprise a large extracellular loop with the N- and C-termini both inserted through the cell membrane. CD36 binds multiple ligands such as thrombospondin, collagen, lipoproteins, and long-chain fatty acids, and has evident roles in the phagocytotic clearance of apoptotic cells, inhibition of angiogenesis, metabolism of glucose and fatty acids, inflammation, and the pathogenesis of malaria. Binding of the FA6-152 antibody to CD36 reportedly blocks its interaction with thrombospondin, collagen, apoptotic cells, and modified LDL, and induces agglutination of fetal but not adult erythrocytes. The epitope for FA6-152 reportedly resides within an immunodominant domain of CD36 comprising amino acids 155 – 183.