Integrin alpha9-beta1 (Y9A2) Mouse Monoclonal Antibody #4703

Integrins are transmembrane glycoproteins that form heterodimers consisting of one α and one β subunit. The dimers act as receptors for extracellular matrix (ECM) proteins at sites of cell adhesion, and interact with focal adhesion (FA) proteins on the cytosolic side, forming the connection between the ECM and the actin cytoskeleton. Signaling to and from integrins regulates cell adhesion, motility, proliferation, apoptosis and gene expression, impacting cellular processes such as development, wound healing, immune response, invasion, metastasis and angiogenesis (reviewed in 1,2). α9β1 integrin is expressed in epithelial cells, smooth and skeletal muscle, neutrophils and hepatocytes (3). Its ligands include the ECM protein tenascin (4) and vascular cell adhesion molecule-1 (VCAM-1) (5). The cytoplasmic domain of α9 integrin binds the focal adhesion adaptor protein, paxillin, inhibiting cell spreading (6,7). Binding of the α9 cytoplasmic domain to spermidine/spermine N(1)-acetyltransferase (SSAT) mediates α9/β1 enhancement of cell migration (8). Physiological functions include development of the lymphatic system (9), possibly through binding to the lymphatic vascular endothelial growth factors VEGF-C and -D (10), neutrophil migration (5), and myogenic differentiation (11).