Product Pathways - PI3K / Akt Signaling
Phospho-GSK-3β (Thr390) Antibody #3548
|3548S||100 µl (10 western blots)||---||In Stock||---|
|3548||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-GSK-3β (Thr390) Antibody detects endogenous levels of human GSK-3β protein only when phosphorylated at Thr390.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr390 of human GSK-3β. Antibodies are purified by peptide affinity chromatography.
Western blot analysis of extracts from HeLa cells, either hydroxyurea-treated (4 mM, 20 hrs) to induce G1/S phase arrest or paclitaxel-treated (100 nM/ml, 20 hrs) for G2/M phase arrest, using Phospho-GSK-3β (Thr390) Antibody (upper) or GSK-3β (27C10) Rabbit mAb #9315 (lower) to show induction of phospho-GSK and equal loading.
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).
The phosphorylation of GSK-3β at Thr390 was found to be a possible substrate of p38 MAPK and was reported by several labs using phosphoproteomic analysis on mitotic cell extracts (6-10). Phosphorylation of this site was also identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for modification site discovery (11). Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.
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- Srivastava, A.K. and Pandey, S.K. (1998) Mol. Cell. Biochem. 182, 135-141.
- Cross, D.A. et al. (1995) Nature 378, 785-789.
- Nusse, R. (1997) Cell 89, 321-323.
- Diehl, J.A. et al. (1998) Genes Dev. 12, 3499-3511.
- Thornton, T.M. et al. (2008) Science 320, 667-70.
- Daub, H. et al. (2008) Mol Cell 31, 438-48.
- Dephoure, N. et al. (2008) Proc Natl Acad Sci USA 105, 10762-7.
- Lowery, D.M. et al. (2007) EMBO J 26, 2262-73.
- Beausoleil, S.A. et al. (2004) Proc Natl Acad Sci USA 101, 12130-5.
- Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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