Lane 1: Hela cell lysate
Lane 2: 293 cell lysate
Lane 3: NIH/3T3 cell lysate
Lane 4: PC-12 cell lysate
Recombinant Rabbit monoclonal primary
GSK3 beta Recombinant Rabbit Monoclonal Antibody [SY28-03] (ET1607-71)
Synthetic peptide within human gsk3 beta aa 360-400.
Hela cell lysate, 293 cell lysate, NIH/3T3 cell lysate, PC-12 cell lysate, Hela, PC-3M, SKOV-3, human breast tissue, human breast carcinoma tissue, mouse testis tissue, mouse prostate 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.
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 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 Alzheimer’s disease. Two forms of GSK-3, designated GSK-3α and GSK-3β, have been identified and differ in their subcellular 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 Alzheimer’s 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 Alzheimer’s disease.
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