Anti-GSK-3α/β (Tyr-279/Tyr-216), Phosphospecific Antibody

Glycogen synthase kinase-3 (GSK-3) has been implicated in fundamental cell processes such as cell fate determination, metabolism, transcriptional control, and oncogenesis. Two GSK-3 genes (α and β) have been cloned in mammals and these kinase homologues show strong sequence conservation within their catalytic domain. GSK-3β plays a critical role in cell survival by phosphorylating nuclear factor-κB (NF-κB) p65 subunit, leading to NF-κB transactivation in hepatocytes. Phosphorylation regulates the activity of both GSK-3 genes. MEK1/2 can phosphorylate tyrosine 216 (tyrosine 279 in GSK-3α), which stimulates GSK-3 kinase activity. Tyr-216 phosphorylation is required for GSK-mediated down-regulation of β-catenin activity. Also, TRAIL stimulation can increase Tyr-216 phosphorylation, and GSK-3β activity may suppress TRAIL-induced apoptosis. Inactiviation of GSK-3 occurs through Akt phosphorylation of serine 9 of GSK-3β (Serine 21 in GSK-3α) . This phosphorylation may be involved in later phases of neuronal apoptosis.

Our GSK-3α/β (Tyr-279/Tyr-216) mouse monoclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat GSK-3α/β (Tyr-279/Tyr-216) and is Protein A purified. It is great for use in WB.

Clone M132 was generated from a phospho-GSK-3β (Tyr-216) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 216 of human GSK-3β. This peptide sequence is also found in GSK-3α (Tyr-279) and is highly conserved in GSK-3 genes in rat and mouse.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects 46/50 kDa* proteins corresponding to the apparent molecular mass of GSK-3β and GSK-3α on SDS-PAGE immunoblots of pervanadate treated rabbit fibroblasts, as well as treated human SKN-SH and A431 cells.