A portion of amino acids 1100-1400 from human Macrophage mannose receptor 1 protein was used as the immunogen for the CD206 antibody.
CD206, also known as macrophage mannose receptor type C (MMR, MRC1L1 and MRC1), is a type I membrane receptor protein. It is an phagocytic and endocytic receptor that can recognize carbohydrate ligands in target molecules. The extracellular portion of the protein includes eight C-type carbohydrate recognition domains (CRD) which are clustered together to achieve higher affinity binding to saccharides. CD206 is found on macrophages and on endothelial cells of the liver and is the only known example of a C-type lectin that contains multiple C-type CRDs. CD206 mediates the endocytosis of glycoproteins by macrophages and binds high-mannose structures on the surface of potentially pathogenic viruses, fungi and bacteria enabling them to be neutralized by phagocytic engulfment. During inflammation, CD206 is crucial for rapid clearance of several mannose-bearing serum glycoproteins but does not regulate the initiation of inflammation. CD206 is primarily expressed in mature tissue macrophages and immature dendritic cells, as well as hepatic and lymphatic endothelial cells, retinal pigmental epithelium (RPE) and mesangial cells.
