Rabbit Polyclonal Antibody
Catalog No. G09-63R
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GSK3α is a multifunctional protein serine kinase, homologous to Drosophila 'shaggy' (zeste-white3) and implicated in the control of several regulatory proteins including glycogen synthase and transcription factors (e.g., JUN) (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 (2).
1. Ali, A. et al: Glycogen synthase kinase-3 : properties, functions, and regulation. Chem. Rev. 101: 2527-2540, 2001.
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.
Recognizes the GSK3α and GSK3β protein
Western blot of GSK3a and GSK3B from human cells
GSK3a and GSK3B from other species may also be detectable.
Synthetic peptide corresponding to amino acids 214-218 of human GSK3β
Store at 4°C (add 0.1% NaN3) for several months, and at -20°C for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For optimal performance, avoid repeated handling and multiple freeze/thaw cycles.
Representative western blot with Anti-GSK3α/β (1:1000) using 20 ng of GST tagged human recombinant GSK3α and GSK3β.
Representative western blot with Anti-GSK3 (1:1000) using 30 μg of HeLa, HEK-293T, and Jurkat cell lysate.
Ishizuka Koko et al., DISC1-dependent switch from progenitor proliferation to migration in the developing cortex Nature April 2011 10.1038/nature09859
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
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
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
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
Douglass Jacqueline et al., Identifying Protein Kinase Target Preferences Using Mass Spectrometry American Journal of Physiology - Cell Physiology June 2012 10.1152/ajpcell.00166.2012
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
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
AKT/PKB Pathway, Cardiovascular Disease, Metabolic Disorder, Neurobiology, Ser/Thr Kinases