This antibody recognizes a 150/130 kDa receptor for fibronectin, (VLA-alpha-5 protein from the integrin superfamily of antigens). It reacts with platelets, lymphocytes, monocytes and most cell lines including K562 and U937.
Integrins are transmembrane glycoproteins that belong to the family of adhesion molecules. They promote interactions between cells and their environment, being both other cells or the extra- cellular matrix. Integrins are a family of heterodimeric membrane glycoproteins consisting of non-covalently associated subunits, i.e. an α-subunit of 95 kDa that is conserved through the superfamily and a more variable β subunit of 150-170 kDa. More than 18 α and 8 β subunits with numerous splice variant isoforms have been identified in mammals. The integrin α5 chain (160 kDa) (CD49e), undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light (25 kDa) and heavy (135 kDa) chains, which non-covalently associate with the integrin β1 subunit (CD29) (130 kDa), thus forming the heterodimer α5-β1 very late antigen (VLA-5) complex. VLA-5 is a fibronectin receptor (FNr) that is expressed on thymocytes, T-cells, monocytes and platelets. It is also found on very early B-cells and activated B-cells. VLA-5 mediates binding of T- and B-cells to fibronectin, an extracellular matrix glycoprotein involved in cell adhesion and migration in wound healing, embryonic development and malignant transformation. The VLA-5 or FNr binds only fibronectin recognizing the Arg-Gly-Asp (RGD) sequence in the central region of the molecule.Synonyms: CD49 antigen-like family member E, FNRA, Fibronectin receptor subunit alpha, Integrin alpha-5, Integrin alpha-F, VLA-5, VLA5