+ +

•  

   

     Western blot analysis of Phospho-beta Catenin (Ser37) in various lysates using Phospho-beta Catenin (Ser37) antibody.    

  
  

Phospho-beta Catenin (Ser37) antibodies are essential tools for studying the regulation and function of beta-catenin, a key effector of the Wnt signaling pathway. Beta-catenin plays dual roles: it stabilizes cell-cell adhesion by interacting with cadherins at the plasma membrane and acts as a transcriptional co-activator in the nucleus to regulate genes involved in cell proliferation and differentiation. Its stability is tightly controlled by the "destruction complex" (APC/Axin/GSK-3β), which phosphorylates beta-catenin at specific residues, including Ser37. priming it for ubiquitination and proteasomal degradation. Phosphorylation at Ser37. mediated by GSK-3β, is a critical regulatory step that marks beta-catenin for turnover, thereby suppressing Wnt pathway activity.

Antibodies targeting phosphorylated Ser37 (p-Ser37) enable researchers to detect this post-translational modification, providing insights into Wnt signaling dynamics. They are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess beta-catenin degradation status in physiological and pathological contexts, such as cancer. In many cancers, Wnt pathway hyperactivation leads to beta-catenin stabilization (non-phosphorylated form) and nuclear accumulation, driving oncogene expression. Monitoring p-Ser37 levels helps evaluate the functional state of the destruction complex and therapeutic responses in preclinical models. These antibodies are often validated for specificity using knockout cells or phosphatase-treated lysates to confirm signal dependence on the Ser37 phosphorylation event. Their application is critical for dissecting mechanisms underlying development, tissue homeostasis, and diseases linked to Wnt/beta-catenin dysregulation.