Anti-GSK-3β (N-terminal region) 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-3β (N-terminal region) mouse monoclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat GSK-3β (N-terminal region) and is Protein A purified. It is great for use in WB, ICC, IHC.

Clone M131 was generated from a recombinant protein containing amino acid residues in the N-terminal region of human GSK-3β. This sequence is highly conserved in rat and mouse GSK-3β, and has 65% homology to similar regions in GSK-3α.

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 a 46 kDa* protein corresponding to the apparent molecular mass of GSK-3β on SDS-PAGE immunoblots of rabbit fibroblasts, mouse brain, as well as human SKN-SH and A431 cells.