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GSK3 beta, Unactive

Recombinant full-length human GSK3beta was expressed in E. coli cells using an N-terminal GST tag.
Catalog No. G09-14G


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Catalog No. Pack Size Price (USD)
G09-14G-20 20 ug $215
G09-14G-50 50 ug $435
G09-14G-BULK BULK Contact Us  


Overview:

GSK3β is a serine threonine protein kinase that was originally identified as the kinase that phosphorylate and inhibits glycogen synthase (1). GSK3β is ubiquitously present in human tissues and implicated in the regulation of several physiological processes, including the control of glycogen and protein synthesis by insulin, modulation of the transcription factors AP-1 and CREB. Transient transfection of human GSK3 beta into Chinese hamster ovary cells stably transfected with individual human tau isoforms leads to hyperphosphorylation of tau at all the sites investigated with phosphorylation-dependent anti-tau antibodies (2).

Genbank Number:


References:


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

2. Sperber BR, Leight S, Goedert M, Lee VM. Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells. Neurosci Lett. 1995 Sep 8;197(2):149-53.


Purity:

Sample Purity Data. For specific information on a given lot, see related technical data sheet.


Storage, Stability and Shipping:

Store product at –70oC. 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.


Molecular Weight:

~75 kDa



Product Datasheets



 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

 Bai Li et al., OLA1 contributes to epithelial-mesenchymal transition in lung cancer by modulating the GSK3β/snail/E-cadherin signaling Oncotarget. March 2016 10.18632/oncotarget.7224

 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

 Richard Rubenstein et al., A novel, ultrasensitive assay for tau: potential for assessing traumatic brain injury in tissues and biofluids Journal of Neurotrauma March 2016 10.1089/neu.2014.3548

 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 IKBα Ubiquitination by Hydrogen Peroxide Journal of Biological Chemistry January 2010 10.1074/jbc.M109.060822

 L Bai et al., OLA1 contributes to epithelial-mesenchymal transition in lung cancer by modulating the GSK3?/snail/E-cadherin signaling Oncotarget March 2016 10.18632/oncotarget.7224

 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

 Martic? Sanela et al., Electrochemical investigations into Tau protein phosphorylations Analyst March 2012 10.1039/c2an35097a

 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

 Gao Feng et al., The Roles of GSK-3? and APC in Cytoplasmic Dynein Regulation Thesis PhD; University of South Carolina December 2014 10.1038/35041020


RESEARCH AREAS

AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, WNT Signaling


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