Glycogen Synthase Kinase 3β (GSK-3β) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/AKT phosphorylates GSK-3β on serine 9, which prevents GSK-3β from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3β is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3β. The phosphorylated serine binds to the GSK-3β priming phosphate position and prevents binding of alternative substrates. In addition to insulin signaling, GSK-3β participates in the Wnt signaling pathway, where it forms a complex with axin, beta-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3β is unable to phosphorylate beta-catenin, which leads to stabilization of beta-catenin. The Wnt pathway inactivates GSK-3β via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3β with axin, beta-catenin, and APC. Clinically, there is considerable interest in GSK-3β inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.
- For Immunocytochemistry, Immunohistochemistry, Western Blot
Recognizes human, mouse, rat, bovine, dog, hamaster, monkey, pig, rabbit and sheep GSK-3alpha/beta. Detects bands of ~51 and ~47kDa by Western blot.
Type: Primary
Antigen: GSK-3ALPHA
Clonality: Monoclonal
Clone: 1H8
Conjugation:
Epitope:
Host: Mouse
Isotype: IgG2b
Reactivity: Human, Mouse, Rat, Sheep (Ovine), Dog (Canine), Pig (Pig, Swine), Monkey, Cow (Bovine), Hamaster, Rabbit