Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
The p190 RhoGAP protein is associated with p120 RasGAP in growth-factor stimulated and tyrosine kinase transformed cells. It functions as a GTPase - activating protein (GAP) for Rho and Rac family proteins, which are involved in regulating cytoskeletal actin and membrane ruffling. The antibody appears to couple signal transduction via Ras and Rho through its association with RasGAP. The presence of two adjacent SH2 domains in the p21 RAS GAP indicates that GAP might interact directly with tyrosine kinases.
p190B can be directly phosphorylated on a single identified tyrosine residue by the activated insulin and IGF-1 receptors. This phosphorylation causes p190B to translocate to the lipid rafts of the plasma membrane, where it can facilitate the inactivation of the Rho GTPase. P190B also has been shown to be tyrosine phosphorylated by cSrc and vSrc. Additionally the GAP domain of p190B is shown to attenuate signal transducing activity of Rac, Rho and CDC42.