Anti-Integrin alphaVbeta5 Antibody, clone P1F6, Phycoerythrin conjugate clone P1F6, from mouse, PE

Integrin alpha-V (UniProt P06756; CD51, Integrin alpha V, Vitronectin receptor subunit alpha) and Integrin beta-5 (UniProt P18084) are encoded by the ITGAV (MSK8, VNRA, VTNR; Gene ID 3685) and the ITGB5 (Gene ID 3693) gene, respectively, in human. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and a beta subunit associated in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence present in the extracellular matrix components, such as fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. The involvement of integrins in vascular proliferation, adhesion, and wound repair has been well documented. Integrin alphaVbeta5 is the primary mechanotransducer that mediates lung myofibroblast contraction-induced latent TGF-beta1 activation. Increased alphaVbeta5 expression is reported to be associated with myofibroblast differentiation. Integrin alphaVbeta5 is shown to interact with Thy-1 in an RLD-dependent manner. Thy-1 expression prevents fibroblast contraction-induced latent TGF-beta1 activation and lung myofibroblast differentiation.