Glycogen synthase kinase 3 alpha (GSK3A) is a serine/threonine protein kinase belonging to the GSK3 family, which includes the closely related isoform GSK3B. GSK3A plays crucial roles in cellular processes such as glycogen metabolism, cell proliferation, differentiation, and apoptosis. Unlike GSK3B, GSK3A has a unique N-terminal extension, but both isoforms share a conserved kinase domain and regulate downstream targets through phosphorylation, often in a primed (phosphorylation-dependent) manner. GSK3A activity is modulated by inhibitory phosphorylation at Ser21. mediated by upstream kinases like AKT, and is implicated in pathways including Wnt/β-catenin, insulin signaling, and neurodevelopment.
Antibodies targeting GSK3A are essential tools for studying its expression, localization, and post-translational modifications. They enable detection in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). Many GSK3A antibodies are designed to distinguish between the phosphorylated (inactive) and unphosphorylated (active) forms, aiding in functional studies. Specificity is critical due to high homology between GSK3A and GSK3B, requiring validation using knockout controls or isoform-specific peptides. Applications span cancer research, neurodegenerative diseases (e.g., Alzheimer’s), and metabolic disorders (e.g., diabetes), where GSK3A dysregulation is linked to pathogenesis. Reliable antibodies support mechanistic insights and therapeutic target validation for small-molecule inhibitors.