Integrin alpha V beta 8 Protein, Human, Recombinant (His)

Integrin alpha V beta 8 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligands. ITGAVB8 does not appear to assume different activation states; and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif; including vitronectin; fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP; which releases active TGF-beta. This mechanism differs from that of alpha V beta 6; the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms.