MUPP1 was first identified as a protein interacting with type 2C serotonin receptor. It acts as a scaffolding protein at tight junctions where it has been reported to interact with integral proteins, anchoring them to the F-actin cytoskeleten. It is also thought to be important in the osmotic stress response in kidney cells and has been shown to play a role in promoting G protein coupling to receptors.
Detection of Mupp1 by Western Blot of Immunprecipitate.
ab101277, at 1 µg/ml, staining Mupp1 in HeLa whole cell lysate immunoprecipitated using ab101277 at 3 µg/mg lysate (1 mg/IP; 20% of IP loaded/lane).
Detection: Chemiluminescence with an exposure time of 3 minutes.