Rat anti Integrin alpha 6A, CD49f

Integrins, are transmembrane glycoproteins that belong to the family of adhesion molecules. They promote interactions between cells and their environment being both other cells and the extra cellular matrix. Integrins are a family of heterodimeric membrane glycoproteins consisting of non-covalently associated subunits, being an ?-subunit of 95 kDa that is conserved through the superfamily and a more variable ? subunit of 150-170 kDa. More than 18 ? and 8 ? subunits with numerous splice variant isoforms have been identified in mammals. One of the integrin alpha subunits is the integrin alpha 6 (?6) subunit. Integrin ?6 (CD49f) primarily associates with the integrin beta 1 (?1) or beta 4 (?4) subunit to form the ?6?1 or laminin receptor and the ?6?4 heterodimer. The GoH3 monoclonal antibody recognizes cell surface antigens on epithelial cells, endothelial cells and in a variety of tissues in both Human and Mouse, and reacts with glycoproteins Ic (?6 integrin, also known as CD49f) complexed with glycoprotein IIa (?1) as the VLA-6 (very late activation antigen) or laminin receptor on Human and Mouse platelets, lymphocytes, epithelial cells and a variety of other cell types. In normal epithelial cells and (colon) carcinoma cells, peripheral nerves, and endothelia however, glycoprotein Ic (?6) is not associated with IIa, but with a group of proteins collectively named ?4. These ?4 proteins can occur in multiple forms on certain cell types. The tumor associated homologue of this protein is the TSP-180 antigen, expressed in lung carcinomas, melanomas, Human tissue carcinomas and carcinoma cell lines but not on Human melanomas and fibroblasts. VLA-6 is expressed on peripheral T cells or thymocytes, the GoH3 monoclonal antibody induces a comitogenic signal and inhibits platelet adhesion to laminin, one of the three major components of the subendothelial matrix.