Anti-Catenin, delta-1 (CTNND1) (pTyr96) Monoclonal Antibody (Clone: 25a)

The membrane associated protein pp120 Src substrate (p120 Catenin, p120cas) was identified as a tyrosine kinase substrate that is phosphorylated in Src transformed cells or in response to growth factor stimulation. It shares structural similarity with the Drosophila Armadillo protein and the vertebrate beta-catenin and gamma-catenin proteins. Its characteristic Arm domain that is composed of 42-amino acid motif repeats evidences this similarity. In the cell, p120 Catenin is localized to the E-Cadherin/catenins cell adhesion complex. Like beta- and gamma-catenin, p120 Catenin directly associates with the cytoplasmic C-terminus of E-Cadherin via its Arm domain and may similarly interact with other Cadherins. It exists as four isoforms that range in size from 90-115kDa. Expression of these isoforms is heterogeneous in human carcinomas, sµggesting that altered pp120 expression contributes to malignancy due to loss of functional cell adhesions. Multiple tyrosine residues (Y96, Y112, Y228, Y280, Y257, Y291, Y296, and Y302) in p120 Catenin are phosphorylated by Src and these phosphorylations may facilitate interaction with PTP1C/SHP-1 in response to EGF stimulation. Thus, p120 Catenin is an Arm domain protein that interacts with both cell adhesion molecules, such as cadherins and cell signaling molecules, such as PTP1C. Protein function: Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476). [The UniProt Consortium]