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REACTIVITY SENSITIVITY MW (kDa)
H Endogenous 46

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.

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Product Usage Information

Application Dilutions
Western Blotting 1:1000

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-GSK-3β (Thr390) Antibody detects endogenous levels of human GSK-3β protein only when phosphorylated at Thr390.


Species Reactivity: Human

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.

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.


1.  Welsh, G.I. et al. (1996) Trends Cell. Biol. 6, 274-279.

2.  Srivastava, A.K. and Pandey, S.K. (1998) Mol. Cell. Biochem. 182, 135-141.

3.  Nusse, R. (1997) Cell 89, 321-323.

4.  Cross, D.A. et al. (1995) Nature 378, 785-9.

5.  Diehl, J.A. et al. (1998) Genes Dev 12, 3499-511.

6.  Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.

7.  Dephoure, N. et al. (2008) Proc Natl Acad Sci U S A 105, 10762-7.

8.  Thornton, T.M. et al. (2008) Science 320, 667-70.

9.  Daub, H. et al. (2008) Mol Cell 31, 438-48.

10.  Lowery, D.M. et al. (2007) EMBO J 26, 2262-73.

11.  Beausoleil, S.A. et al. (2004) Proc Natl Acad Sci U S A 101, 12130-5.


Entrez-Gene Id 2932
Swiss-Prot Acc. P49841


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