https://www.selleckchem.com/products/ted-347.html
Many integrins transmit signals through global conformational changes. However, it is unclear whether integrin αv β8 adopts a similar mechanism during integrin activation and signaling on the cell surface. Here, we showed that disulfide-bonded mutants, which prevented integrin αv β8 lower leg dissociation, bound ligands with similar level as the wild-type protein, suggesting that αv β8 ligand binding did not require lower leg disassociation. We further showed that the N-glycosylation mutant at the interface between the β I and hybrid do
Curtir
Comentario
Compartilhar
