Anti-GSK3B Polyclonal Antibody
應(yīng)用 WB IHC
稀釋比例WB 1:500-2000 IHC 1:50-200.
交叉反應(yīng)Mouse Rat

產(chǎn)品型號：K101564P

更新時間：2022-08-15

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標簽抗體血清球蛋白 IgG Polyclonal Antibody Antibody Monoclonal Antibody 一抗內(nèi)參抗體膠體金標記二抗生物素化二抗 RBITC熒光標記抗體二抗 FITC熒光標記抗體二抗免疫血清二抗純化抗體二抗 HRP標記二抗免疫球蛋白抗原IgG二抗

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Anti-GSK3B Polyclonal Antibody

英文名稱	Anti-GSK3B Polyclonal Antibody
宿主	Rabbit
別名	GSK-3 beta;Glycogen Synthase Kinase 3 Beta;GSK3beta isoform;Serine/threonine-protein kinase GSK3B
應(yīng)用	WB IHC
稀釋比例	WB 1:500-2000 IHC 1:50-200.
交叉反應(yīng)	Mouse Rat
蛋白分子量	47kDa
Gene ID	2932
保存	Store at -20°C. Avoid freeze / thaw cycles.
儲存液	Buffer: PBS with 0.03% Proclin300, 50% glycerol, pH7.3.
純化方法	Affinity purification
亞型	IgG
免疫原	A synthetic peptide of human GSK3B
性狀	液體
Public Immunogen Range	A synthetic peptide of human GSK3B
Subcellular Locations	Cell membrane Cytoplasm Nucleus
Swiss Prot	P49841
克隆類型	Polyclonal Antibody
背景資料	Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, 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 insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates 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 multimeric 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 regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates 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 regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through 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. Regulates 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 regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation.