Issues associated with assessing nuclear localization of N-terminally unphosphorylated β-catenin with monoclonal antibody 8E7

Issues associated with assessing nuclear localization of N-terminally unphosphorylated β-catenin with monoclonal antibody 8E7

Biology Direct, February 2009

19187541

Meghan T Maher, Annette S Flozak, Alyssa M Hartsell, Susan Russell, Rohinee Beri, Ofra N Peled, Cara J Gottardi

Beta-catenin is a dual function adhesion/transcriptional co-activator protein, and both functions are critical for normal tissue homeostasis. Since the transcriptional functions of beta-catenin are more often implicated in various disease processes, there is much interest in the development and use of reagents to interrogate spatial and temporal evidence of beta-catenin nuclear signaling in cells and tissues. An important study demonstrated that the signaling form of beta-catenin is specifically unphosphorylated at residues S37 and T41, and suggested that this form exhibits a propensity for cytosolic/nuclear accumulation relative to the total pool of beta-catenin.