Species predicted to react based on 100% sequence homology:Mouse, Rat, Monkey
Specificity / Sensitivity
Phospho-Catenin δ-1 (Ser320) Antibody recognizes endogenous levels of catenin δ-1 protein only when phosphorylated at Ser320.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser320 of human catenin δ-1 protein. Antibodies are purified by protein A and 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).
Phosphorylation at Ser320 on catenin δ-1 was identified at Cell Signaling Technology (CST) using PhosphoScan®, a CST™ LC-MS/MS platform for phosphorylation site discovery (5).