Enzymes, Signaling Proteins, Extracellular Ligands, Signaling Reagents, Antibodies

Catalog No.	Pack Size	Price (USD)
G09-652R-100	100 ul	$715
G09-652R-BULK	BULK	Contact Us

Overview:

Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase that is involved in the regulation of many signaling pathways. There have been two isoforms identified, GSK3alpha and GSK3beta. GSK3beta is ubiquitously expressed in human tissues and is implicated in regulating several physiological processes. These include the control of glycogen, protein synthesis by insulin and modulation of the transcription factors AP-1 and CREB. GSK3beta has been shown to play a key inhibitory role in both the insulin and Wnt signaling pathways (1). GSK3beta is inhibited by phosphorylation at Ser9. Insulin signaling is largely responsible for this mode of GSK3beta inhibition (2).

References:

1. Papkoff, J. et al: WNT-1 and HGF regulate GSK3b activity and beta catenin signaling in mammary epithelial cells. Biochem Biophys Res Commun. 1998 Jun 29;247(3):851-8.

2. Sutherland, C. et al: Inactivation of glycogen synthase kinase 3 beta by phosphorylation: new kinase connections in insulin and growth factor signaling. Biochem J. 1993 Nov 15; 296 (Pt. 1):15-9.

Specificity:

Recognizes the GSK3 beta protein phosphorylated at serine 9

Cross Reactivity:

Human, Mouse, Rat, Chicken, Bovine, Canine, non-Human Primate, Xenopus and Zebrafish

Host:

Rabbit, IgG

Immunogen:

Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 conjugated to KLH

Purification:

Affinity Chromatography

Stability:

Store at 4^oC (add 0.1% NaN₃) for several months, and at -20^oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Sample Data:

Western blot of rat cortex lysate showing specific immunolabeling of the ~46kDa GSK3 beta protein phosphorylated at Ser9 (control). Immunolabeling is blocked by the phospho-peptide (peptide) used as antigen but not by the corresponding dephosphopeptide (not shown).

Product Datasheets

J1274-17

Ishizuka Koko et al., DISC1-dependent switch from progenitor proliferation to migration in the developing cortex Nature April 2011 10.1038/nature09859

Tang Wenwen et al., A PLCβ/PI3Kγ-GSK3 Signaling Pathway Regulates Cofilin Phosphatase Slingshot2 and Neutrophil Polarization and Chemotaxis Developmental Cell December 2011 10.1016/j.devcel.2011.10.023

I Pronobis Mira et al., A novel GSK3-regulated APC:Axin interaction regulates Wnt signaling by driving a catalytic cycle of efficient ?catenin destruction Elife September 2015 10.7554/eLife.08022

Li Saiqun et al., GSK3 Temporally Regulates Neurogenin 2 Proneural Activity in the Neocortex Journal of Neuroscience November 2012 10.1523/JNEUROSCI.1309-12.2012

FJ Gao et al., GSK-3β Phosphorylation of Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters Dynein Motility. Traffic September 2015 10.1111/tra.12304

JN Kong et al., Regulation of Chlamydomonas flagella and ependymal cell motile cilia by ceramide-mediated translocation of GSK3. Molecular Biology of the Cell December 2015 10.1091/mbc.E15-06-0371

S. Desai Shruti et al., GSK-3β Protein Phosphorylates and Stabilizes HLXB9 Protein in Insulinoma Cells to Form a Targetable Mechanism of Controlling Insulinoma Cell Proliferation Journal of Biological Chemistry January 2014 10.1074/jbc.M113.533612

Yamaguchi Fuminori et al., S100 Proteins Modulate Protein Phosphatase 5 FunctionA LINK BETWEEN CA2+ SIGNAL TRANSDUCTION AND PROTEIN DEPHOSPHORYLATION Journal of Biological Chemistry April 2012 10.1074/jbc.M111.329771

Banerjee Sami et al., Modulation of SCFβ-TrCP-dependent I_KBα Ubiquitination by Hydrogen Peroxide Journal of Biological Chemistry January 2010 10.1074/jbc.M109.060822

D Xu et al., Obg-like ATPase 1 regulates global protein serine/threonine phosphorylation in cancer cells by suppressing the GSK3β-inhibitor 2-PP1 positive feedback loop. Oncotarget January 2016 10.18632/oncotarget.6496

Martic Sanela et al., Electrochemical Investigations of Tau Protein Phosphorylations and Interactions with Pin1 Chemistry & Biodiversity September 2012 10.1002/cbdv.201100418

Villanueva JO Esteves et al., Electrochemical detection of anti-tau antibodies binding to tau protein and inhibition of GSK-3β-catalyzed phosphorylation. Analytical Biochemistry March 2016 10.1016/j.ab.2015.12.002

S. Darshita B et al., Identification and in vitro evaluation of new leads as selective and competitive glycogen synthase kinase-3β inhibitors through ligand and structure based drug design Journal of Molecular Graphics and Modelling July 2014 10.1016/j.jmgm.2014.06.013

Anti-phospho-GSK3 beta (Ser9)

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