Description
Product Characteristics:
Two families of mammalian lectin-like adhesion molecules bind glycoconjugate ligands in a sialic acid-dependent manner: the selectins and the sialoadhesins. The sialic acid-binding immunoglobulin superfamily lectins, designated siglecs or sialoadhesins, are immunoglobulin superfamily members recognizing sialylated ligands. The common sialic acids of mammalian cells are N-acetyl-neuraminic acid (Neu5Ac) and N-glycolyl-neuraminic acid (Neu5Gc). Siglec-1 mediates local cell-cell interactions in lymphoid tissues and can be detected at contact points of macrophages with other macrophages, sinus-lining cells and reticulum cells. Siglec-7, highly expressed in monocytes and resident blood cells, but not in parenchymatous cells, mediates inhibition of natural killer cell cytotoxicity. Siglec-9 is closely homologous to Siglec-7, the gene encoding it maps to chromosome 19q13.41 in humans. It is highly expressed in peripheral blood leukocytes (but not eosinophils), liver, bone marrow, placenta and spleen. Siglec-8, a type I membrane protein, is selectively expressed on human eosinophils, basophils and mast cells, where it regulates their function and survival.
Subcellular location: Extracellular
Synonyms: CD329, CDw329, OB binding protein like, OBBP LIKE, Protein FOAP 9, Protein FOAP-9, sialic acid binding Ig like lectin 9, Sialic acid-binding Ig-like lectin 9, Sialic acid-binding immunoglobulin like lectin 9, SIGL9_HUMAN, Siglec 9, Siglec-9, SIGLEC9.
Target Information: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules