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Glycogen synthase kinase-3 (GSK3), originally discovered as a serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase, is now known to regulate a diverse array of cellular processes. Inappropriate regulation of GSK3 signaling is thought to play a role in the development of type II diabetes mellitus, neuronal cell loss in Alzheimer’s disease and cancer. The two major isoforms of GSK3 in mammalian tissues (GSK3α and 3β) are structurally similar but not functionally equivalent. GSK3β activity is relatively high in resting cells, and it can be positively or negatively regulated by various stimuli. GSK3β is a promising drug target and high-throughput study methods are in demand.
Figure 1: Measurement of phosphorylated and total GSK3β.
NIH/3T3 cells were cultured in 96-well plates and serum-starved for 16 hours. Cells were then treated with 20% FBS for 30 minutes and fixed. Total and phospho GSK3β were each assayed in triplicate using the phospho and total GSK3β antibodies included in the FACE GSK3β Kit. Data was plotted after correction for cell number (performed through use of Crystal Violet).
Antibody Specificities
The phospho-GSK3β antibody was raised in rabbit against a synthetic phospho-peptide corresponding to the sequence surrounding serine 9 of human GSK3. This antibody recognizes phosphorylated GSK3β only when phosphorylated at this site and does not recognize phosphorylated GSK3α. The total-GSK3β antibody recognizes GSK3β proteins regardless of the phosphorylation state.
