ELISA GSK3B Antibody, FITC

Quantity :50µg Clone Number: Aliases:Glycogen Synthase Kinase 3 Beta antibody; Glycogen synthase kinase-3 beta antibody; GSK 3 beta antibody; GSK-3 beta antibody; GSK3B antibody; GSK3B_ antibody; GSK3beta isoform antibody; Serine/threonine-protein kinase GSK3B antibody Product Type:Polyclonal Antibody Immunogen Species:Homo sapiens () UniProt ID:P49841 Immunogen:Recombinant Glycogen synthase kinase-3 beta protein (1-420AA) Raised in:Rabbit Reactivity: Tested Applications: Background:Constitutively active protein kinase that acts as a negative regµLator in the hormonal control of glucose homeostasis, Wnt signaling and regµLation of transcription factors and microtubµLes, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insµLin regµLation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insµLin resistance by regµLating activation of transcription factors. RegµLates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a mµLtimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regµLation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubµLes. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubµLes at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubµLes which is critical for its role in bµLge stem cell migration and skin wound repair. Probably regµLates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regµLates replication in pancreatic beta-cells, resµLting in apoptosis, loss of beta-cells and diabetes. Throµgh phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. RegµLates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regµLates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Clonality:Polyclonal Isotype:IgG Purification Method:>95%, Protein G purified Conjµgate:FITC Buffer:Preservative: 0.03% Proclin 300 Constituents: 50% Glycerol, 0.01M PBS, PH 7.4 Form:Liquid Stroage:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Target Names:GSK3B Research Areas:Neuroscience; Cancer; CardiovascµLar; Metabolism; Signal transduction; Stem cells