M-RIP polyclonal antibody

Myosin phosphatase-rho interacting protein (M-RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin-myosin filaments regulating cytoskeletal dynamics. M-RIP contains amino-terminal pleckstrin homology domains, carboxyl-terminal coiled-coil domains, and was originally identified to associate with the myosin phosphatase complex. M-RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA. Phosphorylation of MYRT by Rho-associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractility. M-RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin. Silencing of M-RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of M-RIP polyclonal antibody at 1:5000 dilution Lane1:PC12 whole cell lysate (40ug) Lane2:CT-26 whole cell lysate (40ug) Lane3:H1792 whole cell lysate (40ug) Lane4:Myla2059 whole cell lysate (40ug) Lane5:PC3 whole cell lysate (40ug) Lane6:SGC7901 whole cell lysate (40ug)