Description
Recombinant full-length human Catenin alpha was expressed by baculovirus in Sf9 insect cells using a N-terminal GST tag.
Scientific Background: Catenin alpha is a novel actin-binding and -bundling protein. Catenin alpha is responsible for organizing and tethering actin filaments at the zones of E-cadherin-mediated cell-cell contact (1). Monomeric Catenin alpha can bind strongly to E-Cadherin-beta-Catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that Catenin alpha is an allosteric protein. Catenin alpha directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments (2)