Western blot of rat cortex lysate showing specific immunolabeling of the ~46 kDa GSK3ß protein phosphorylated at Ser9 (control). Immunolabeling is blocked by the phospho-peptide (peptide) used as the antigen but not by the corresponding dephosphopeptide (not shown).
|Tested species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 of rat GSK3B conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1/1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody is predicted to react with human, mouse, chicken, bovine, canine, non-human primate, zebrafish and Xenopus based on 100% sequence homology.
In Western blot, this antibody is specific for the ~46kDa GSK3 beta protein phosphorylated at Ser9. It also weakly labels the ~51 kDa GSK3a band due to the high degree of homology between the 2 subunits. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide.
Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase that is involved in the regulation of many signaling pathways. To date, 2 isoforms have been identified: GSK3a and GSK3ß. Specifically, GSK3ß has been shown to play a key inhibitory role in both the insulin and Wnt signaling pathways (Papkoff and Aikawa 1998). It has been suggested that Ser9 phosphorylation underlies the inhibition of GSK3ß by insulin (Sutherland et al., 1993).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.