Glycogen synthase kinase-3 α and β (GSK-3α, β) are serine/threonine kinases that regulate metabolic enzymes and transcription factors, which are responsible for coordinating processes such as glycogen synthesis and cell adhesion. GSK-3β activity is also required for nuclear activity of Rel dimers, which mediate an anti-apoptotic response to TNFα in mice. GSK-3 catalytic kinase activity is controlled through differential phosphorylation of serine/threonine residues, which have an inhibitory effect, and tyrosine residues, which have an activating effect. Growth factor stimulation of mammalian cells expressing GSK-3α and GSK-3β induces phosphorylation of Ser 21 and Ser 9, respectively through a phosphatidylinositol 3-kinase (PI 3-kinase)-protein kinase B (PKB) dependent pathway, thereby enhancing proliferative signals. Additionally, GSK-3 physically associates with cAMP-dependent protein kinase A (PKA), which phosphorylates Ser 21 of GSK-3α or Ser 9 of GSK-3β and inactivates both forms

Glycogen synthase kinase-3 alpha; GSK-3 alpha; Serine/threonine-protein kinase GSK3A; GSK3A

p49840/p49841

Human,Mouse,Rat

WB,IHC

WB 1:500-1:2000
IHC 1:50-1:200

~ 46,51 kDa

Rabbit

This antibody detects endogenous levels of GSK3α/β protein only when phosphorylated at Tyr279/216

Synthetic phosphopeptide derived from human GSK3α around the phosphorylation site of Tyrosine 279.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.