Clone REA153 recognizes the threonine residue (T310)-phosphorylated form of p120 Catenin, a prototypic member of subfamily of Armadillo-domain (ARM) proteins. p120 ARM domain displays 22% homology to other ARM-domain proteins such as β-catenin and plakoglobin, which are basically cadherin binding proteins, suggesting the involvement of p120 in binding to cadherin. p120 associates with most classical (type I) and nonclassical (type II) cadherins via ARM repeats 1–7 and is localised at the cell junctions, where it constitutes the cadherin complex. Functions of p120 include regulation of stability of cadherins and modulation of activity of rho GTPases in the cytoplasm. Furthermore, lack of p120 Catenin in mouse leads to tumor development, suggesting its further role as tumor supressor. Phosphorylation of p120 Catenin at multiple sites regulates its various functions and it can be phosphorylated by Src and various receptor tyrosine kinases. 

Additional information: Clone REA153 displays negligible binding to Fc receptors.