Lane 1: Hela cell lysate
Lane 2: A549 cell lysate
Recombinant Rabbit monoclonal primary
Phospho-GSK3 beta (Ser 9) Recombinant Rabbit Monoclonal Antibody [SY02-71] (ET1607-60)
Synthetic phospho-peptide corresponding to residues surrounding ser9 of human gsk3 beta.
Hela cell lysate, A549 cell lysate, Hela, MCF-7, human colon carcinoma tissue, human breast tissue, human breast carcinoma tissue, human kidney tissue, human pancreas tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Phospho-GSK3 beta (Ser 9)
Glycogen Synthase Kinase 3 Beta antibody; Glycogen synthase kinase-3 beta antibody; GSK 3 beta antibody; GSK-3 beta antibody; GSK3B antibody; GSK3B_HUMAN antibody; GSK3beta isoform antibody; Serine/threonine-protein kinase GSK3B antibody
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Expressed in testis, thymus, prostate and ovary and weakly expressed in lung, brain and kidney. Colocalizes with EIF2AK2/PKR and TAU in the Alzheimer disease (AD) brain.
Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and desactivates GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216. Inactivated by phosphorylation at Ser-9 (Probable). Phosphorylated in a circadian manner in the hippocampus (By similarity).; Mono-ADP-ribosylation by PARP10 negatively regulates kinase activity.
Cytoplasm, Nucleus, Cell membrane.
Glycogen 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.