Catenins have emerged as molecular sensors that integrate cell-cell junctions and cytoskeletal dynamics with signaling pathways that control morphogenesis and cell to cell communication. delta1-Catenin (p120 catenin) is a catenin family member which contains an N-terminal coiled-coil domain, a regulatory domain containing multiple phosphorylation sites, and a central Armadillo repeat domain. delta1-Catenin regulates E-cadherin turnover, and has both positive and negative effects on cadherin-mediated adhesion. Actin dynamics are also regulated by delta1-Catenin, which can modulate RhoA, Rac and cdc42 activity. delta1-Catenin is phosphorylated at multiple tyrosine, serine and threonine sites both in vitro and in vivo. High levels of delta1-Catenin phosphorylated at Tyr-228 are commonly seen in several carcinoma cell lines and after EGFR activation. Many other tyrosine sites are also phosphorylated in the N-terminal region including Tyr-96, Tyr-112, Tyr-280, and Tyr-302. In addition, Thr-310 and Thr-916 are constituitively phosphorylated in many cell types, however this phosphorylation may occur only in delta1-Catenin associated with the plasma membrane.
Clone M356 was generated from a phospho-delta1-Catenin (Tyr-228) synthetic peptide containing amino acid residues around tyrosine 228 of human delta1-Catenin.
Target:
delta1-Catenin (Tyr-228)
Application Dilute:
WB(1:300-5000)
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