Mouse anti Integrin alpha 5 (CD49e) from MyBioSource.com

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 alpha-subunit of 95 kDa that is conserved through the superfamily and a more variable beta subunit of 150-170 kDa. More than 18 alpha and 8 beta subunits with numerous splice variant isoforms have been identified in mammals. The integrin alpha5 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 beta1 subunit (CD29) (130 kDa), thus forming the heterodimer alpha5-beta1 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