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GSK-3 Fusion Protein #9237
AKT Kinase activity of PDGF-treated NIH/3T3 cell extracts was analyzed by IP/Kinase assay. Cell extracts (200 μl) were incubated overnight with Immobilized Phospho-Akt (Ser473) (D9E) Rabbit mAb #4070. After extensive washing the kinase reaction was performed in the presence of 200 μM of cold ATP and 1 μg of GSK-substrate. Phosphorylation of GSK-3 was measured by Western blot using Phospho-GSK-3 a/β (Ser21/9) Antibody #9327.Learn more about how we got this image
Gallery: GSK-3 Fusion Protein #9237
GSK-3 Fusion Protein serves as a useful substrate for assaying Akt kinase activity. It is expressed as a protein fusion to the GSK-3 α/β crosstide, corresponding to residues surrounding GSK-3 α/β (Ser21/9) (CGPKGPGRRGRRRTSSFAEG).
Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).
Protein Specific References
For Research Use Only. Not For Use In Diagnostic Procedures. Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.