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.
Molecular Weight:
187.95 kDa (predicted)
Purity:
96.80%
TMPY-05717
* VAT and and shipping costs not included. Errors and price changes excepted