Anti-Phospho-GSK3 beta (S9) Antibody [SY02-71]

HUABIO

Anti-Phospho-GSK3 beta (S9) Antibody [SY02-71]

7

Flow Cytometry, ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin

WB,IF-Cell,IF-Tissue,IHC-P

Research Use Only

Monoclonal

SY02-71

1 mg/ml

Unconjugated

GSK3B

glycogen synthase kinase 3 beta

glycogen synthase kinase-3 beta, GSK-3 beta, serine/threonine-protein kinase GSK3B

Rabbit

IgG

Glycogen synthase kinase-3 beta

Glycogen synthase kinase-3alpha (GSK-3alpha) and GSK-3beta 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-3beta activity is also required for nuclear activity of Rel dimers, which mediate an anti-apoptotic response to TNFalpha 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-3alpha and GSK-3beta 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-3alpha or Ser 9 of GSK-3beta and inactivates both forms. GSK-3alpha/beta is positively regulated by phosphorylation on Tyr 279 and Tyr 216, respectively. Activated GSK-3alpha/beta participates in energy metabolism, neuronal cell development, and body pattern formation. Tyrosine dephosphorylation of GSK-3 is involved in its extracellular signal-dependent inactivation.

Human

Human

-20°C,2°C to 8°C

41116161