|Reactivity:||Hu, Ms, Rt|
Western blotting 1:1000 Immunohistochemistry 1:100 Immunofluorescence (IF-IC) 1:200
|Purification:||Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser9 of human GSK-3beta|
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 phosphory-lates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3 kinase/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3a and Ser9 of GSK-3beta (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).Phospho-GSK-3beta (Ser9) (D85E12) Rabbit mAb detects endogenous levels of GSK-3beta only when phosphorylated at Ser9. This antibody reacts with denatured components of bovine serum, including BSA.
|Buffer:||Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA, 50% glycerol and less than 0.02% sodium azide.|
|Storage:||at 4-8 °C for short term, at -20°C for longer term.|
Western blot analysis of extracts from PC-3 cells, untreated or LY294002/wortmannin-treated, using Phospho-GSK-3beta (Ser9) (Rabbit mAb (upper) or GSK-3beta Rabbit (lower).
Immunohistochemical analysis of paraffin embedded human breast carcinoma tissue using Phospho GSK3B – S9 antibody
Western blot analysis of extracts from GSK-3a (-/-) (lanes 1,2) and GSK-3beta (-/-) (lanes 3,4) mouse embryonic fibroblast (MEF) cells, λ phosphatase or PDGF-treated, using Phospho-GSK-3beta(Ser9) (Rabbit mAb (upper) and a/beta-Tubulin Antibody (lower).
Immunofluorescence staining of methanol-fixed Hela Cells showing cytoplasmic staining using Phospho-GSK3B-S9 antibody
(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) Cross, D.A. et al. (1995) Nature 378, 785-789. (4) Nusse, R. (1997) Cell 89, 321-323. (5) Diehl, J.A. et al. (1998) Genes Dev. 12, 3499-3511.