Integrins are a family of proteins that mediate intercellular adhesion or adherence to extracellular matrix proteins. Their roles are essential for embryonic development, tumor metastasis, organ function, and proper immune cell function. Family members are heterodimers that contain a larger α subunit that is unique to each individual receptor and a smaller β subunit that can be shared by several receptors. Based on β subunit content, integrins are divided into the subfamilies β1, β2, and β3. The β3 subfamily contains the vitronectin receptor (αVβ3) and the platelet protein gpIIb/IIIa. The α chain of the vitronectin receptor (VNRα, CD51, integrin αV) has been reported to consist of a disulfide-linked large extracellular (125 kDa) subunit and a smaller (25 kDa) membrane-anchored subunit. The large subunit contains multiple sequences with homology to calcium-binding sites in other proteins and an RGD-dependent ligand-binding site, while the small subunit contains a transmembrane domain and a short cytoplasmic domain. VNRα has been reported to be noncovalently associated with the VNR β3-chain (CD61, gpIIIa). The VNR mediates cell adhesion to RGD-containing ligands such as vitronectin, von Willebrand factor, fibrinogen, and thrombospondin.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.