Glycogen synthase kinase 3, or GSK-3, is a serine/threonine, proline-directed kinase involved in a diverse array of signaling pathways, including glycogen synthesis and cellular adhesion, and has been implicated in Alzheimers disease. Two forms of GSK-3, designated GSK-3alpha and GSK-3beta, have been identified and differ in their subcel lular localization. Tau, a microtubule-binding protein which serves to stabilize microtubules in growing axons, is found to be hyper-phosphorylated in paired helical filaments (PHF), the major fibrous component of neurofibrillary lesions associated with Alzheimers disease. Hyperphosphorylation of Tau is thought to be the critical event leading to the assembly of PHF. Six Tau protein isoforms have been identified, all of which are phosphorylated by GSK-3. This presents the possibility that miscues in GSK-3 signaling contribute to the onset of Alzheimers disease.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IP: 1:50~1:200
Application Notes:
GSK3alpha (G15) polyclonal antibody detects endogenous levels of GSK3alpha protein.
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