The Phospho-delta 1 Catenin (Thr916) antibody is designed to detect delta-catenin (δ-catenin), a member of the p120-catenin subfamily, specifically phosphorylated at threonine 916. Delta-catenin plays a critical role in cell-cell adhesion by binding to the juxtamembrane domain of classical cadherins, stabilizing adherens junctions, and regulating cytoskeletal dynamics. Its phosphorylation at Thr916 is a post-translational modification implicated in modulating protein-protein interactions, cellular signaling, and subcellular localization. This site is thought to be targeted by kinases involved in pathways such as Wnt or receptor tyrosine kinase (RTK) signaling, which influence cell migration, proliferation, and polarity.
The antibody is widely used in research to investigate the regulatory mechanisms of delta-catenin in physiological and pathological contexts, including cancer and neurological disorders. For example, aberrant delta-catenin phosphorylation has been linked to tumor progression, neuronal development, and synaptic plasticity. By enabling the specific detection of Thr916 phosphorylation, this tool helps elucidate how post-translational modifications regulate delta-catenin’s dual roles in adhesion and signaling. Applications include Western blotting, immunofluorescence, and immunoprecipitation in cell or tissue samples. Validation often involves comparing phosphorylated and non-phosphorylated states or using kinase/phosphatase inhibitors to confirm specificity. Its utility extends to studies exploring therapeutic targets in diseases with disrupted cell adhesion or signaling pathways.