+ +

•  

   

     Western blot analysis of Phospho-GSK3 (Tyr279/Tyr216) in 293 lysates using Phospho-GSK3 alpha/beta (Tyr279/Tyr216) antibody.    

  
  

•  

   

     Immunofluorescence analysis of Phospho-GSK3 (Tyr279/Tyr216) in Hela cells using GSK3a/b(Phospho-Tyr279/216) antibody(red).    

  
  

•  

   

     Immunohistochemistry analysis of paraffin-embedded Human breast carcinoma tissue using Phospho-GSK3 (Tyr279/Tyr216) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval. Sample with blocking peptide on the right.    

  
  

The Phospho-GSK3 (Tyr279/Tyr216) antibody is a critical tool for studying the regulation and activity of Glycogen Synthase Kinase 3 (GSK3), a serine/threonine kinase with two isoforms, GSK3α and GSK3β. GSK3 plays a central role in cellular processes, including metabolism, proliferation, and apoptosis, by modulating key signaling pathways such as Wnt, insulin, and growth factor signaling. Its activity is tightly regulated by phosphorylation at specific residues.

In its inactive state, GSK3 is phosphorylated at an N-terminal serine residue (Ser21 in GSK3α, Ser9 in GSK3β), which suppresses its kinase activity. Conversely, phosphorylation at tyrosine residues Tyr279 (GSK3α) and Tyr216 (GSK3β) enhances catalytic activity. These phosphorylation events are mediated by autophosphorylation or upstream kinases, promoting substrate recognition and kinase activation. The Phospho-GSK3 (Tyr279/Tyr216) antibody specifically detects these phosphorylated tyrosine residues, enabling researchers to assess GSK3 activation status in various contexts.

This antibody is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate GSK3 dynamics in diseases such as neurodegenerative disorders, cancer, and diabetes. Dysregulated GSK3 activity has been linked to pathologies like Alzheimer’s disease (via tau hyperphosphorylation) and tumor progression, making this antibody a valuable tool for mechanistic and therapeutic studies. Its specificity for active GSK3 helps clarify phosphorylation-dependent signaling crosstalk and drug targeting strategies.