mouse monoclonal IgG2b; Integrins are heterodimers composed of noncovalently associated transmembrane α and β subunits. The sixteen α and eight β subunits heterodimerize to produce more than 20 different receptors. Most integrin receptors bind ligands that are components of the extracellular matrix, including Fibronectin, collagen and Vitronectin. Certain integrins can also bind to soluble ligands such as fibrinogen, or to counter-receptors on adjacent cells such as the intracellular adhesion molecules (ICAMs), leading to aggregation of cells. Ligands serve to cross-link or cluster integrins by binding to adjacent integrin receptors; both receptor clustering and ligand occupancy are necessary for the activation of integrin-mediated responses. In addition to mediating cell adhesion and cytoskeletal organization, integrins function as signaling receptors. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis. Integrin α2 is responsible for adhesion of platelets and other cells to collagens. Modulation of collagen and collagenase gene expression force generation and organization of newly synthesized extracellular matrix.