Catenin delta-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function. Catenin delta-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion. Catenin delta-1 has both positive and negative effects on cadherin-mediated adhesion. Actin dynamics are also regulated by catenin delta-1, which modulates RhoA, Rac, and cdc42 proteins. Analogous to beta-catenin, catenin delta-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin delta-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin delta-1 may function as a tumor suppressor.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
Catenin-delta1 (phospho-Y228) polyclonal antibody detects endogenous levels of Catenin-delta1 protein only when phosphorylated at Tyr228.
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