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Integrins are heterodimeric transmembrane receptors that mediate cell-cell or cell-matrix adhesion. They contain noncovalently associated α and β subunits that consist of a large extracellular region (the ligand-binding domain), a short transmembrane region, and a cytoplasmic domain of varying length. In mammals, at least 17 α subunits and 8 β subunits have been identified and these proteins can heterodimerize to form at least 22 different receptors. Although there is a high degree of redunancy, each integrin has a specific biological function. For example, the β3 subunit associates with αIIb in platelets where this glycoprotein complex acts as a fibrinogen receptor and mediates platelet aggregation. In endothelial cells (EC), β3 complexes with the αv subunit to form the vitronectin receptor. This receptor mediates endothelial cell adhesion to vitronectin, fibrinogen, von Willebrand factor, thrombospondin, laminin, and fibronectin. In confluent EC cultures, the αvβ3 integrin localizes to focal adhesions at the cell body and cell-cell borders. Thus, continued study of individual integrin subunits will provide insights to mechanisms of cell adhesion and signaling.Host Species: MouseClone: 1Isotype: IgG1Species Reactivity: HumanImmunogen: Human Integrin β3 aa. 592-712Formula Weight [Chemical]: 104kDaImmunofluorescence, Western Blotting
