GSK-3 Fusion Protein serves as a useful substrate for assaying Akt kinase activity.
Molecular Weight: 30 kDa
GSK-3 fusion protein at a concentration of 1ug/40uL reaction is phosphorylated by an upstream kinase in an in vitro kinase assay with 1X kinase buffer #9802 and 200uM ATP #9804. After a 30 minute assay at 30C, phosphorylation can be detected using a phospho-GSK3 antibody.
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).
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