Phospho-Catenin δ-1 (Tyr228) Antibody detects endogenous levels of catenin δ-1 protein only when phosphorylated at Tyr228. The antibody might cross react with another overexpressed phospho-tyrosine protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Tyr228 of human/mouse catenin δ-1. Antibodies are purified by peptide affinity chromatography.
Background
Catenin δ-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 (1). Catenin δ-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 (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).Catenin δ-1 is phosphorylated at multiple tyrosine sites along its sequence both in vivo and in vitro (5). High levels of catenin δ-1 phosphorylated at Tyr228 are commonly seen in several carcinoma cell lines. EGFR signaling induces catenin δ-1 phosphorylation at Tyr228, with the phosphorylated protein becoming localized at adherens junctions although phosphorylation is not essential in junction formation (6).
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