Phospho-GSK3 beta (Ser 9) Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of Phospho-GSK3 beta(Ser 9) on different lysates using anti-Phospho-GSK3 beta(Ser 9) antibody at 1/1,000 dilution.
Lane 1: Hela
Lane 2: MCF-7
Fig2: ICC staining Phospho-GSK3 beta(Ser 9) in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Fig3: ICC staining Phospho-GSK3 beta(Ser 9) in MCF-7 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Host Species; Species ReactivityRabbit; Human
ImmunogenSynthetic phospho-Peptide corresponding to residues surrounding Ser9 of human GSK3 beta.
Application SummaryWB, ICC/IF, IHC
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesGlycogen synthase kinase-3 beta, Serine/threonine-protein kinase GSK3B
BackgroundGlycogen synthase kinase-3α (GSK-3α) and GSK-3β are highly similar isoforms of 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-K)-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. GSK-3α/β is positively regulated by phosphorylation on Tyr 279 and Tyr 216, respectively. Activated GSK-3α/β participates in energy metabolism, neuronal cell development, and body pattern formation. Tyrosine dephosphorylation of GSK-3 is involved in its extracellular signal-dependent inactivation.(ET1607-60)