GSK-3α Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P49840 |
Other Accession | NP_063937 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 50981 Da |
Gene ID | 2931 |
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Positive Control | Western Blot: 3T3 cell lysate |
Application & Usage | Western blot: 1-4 µg |
Other Names | Serine/threonine-protein kinase GSK3A, GSK-3alpha, Glycogen synthase kinase-3, GSK-3 alpha |
Target/Specificity | GSK-3α |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | 100 µg (0.5 mg/ml) of GSK-3α antibody in PBS pH 7.2, 0.01 % BSA, 0.01 % thimerosal, and 50 % glycerol. |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | GSK-3α Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | GSK3A |
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Function | 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), CTNNB1/beta-catenin, APC and AXIN1 (PubMed:11749387, PubMed:17478001, PubMed:19366350). Requires primed phosphorylation of the majority of its substrates (PubMed:11749387, PubMed:17478001, PubMed:19366350). Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:11749387, PubMed:17478001, PubMed:19366350). Regulates glycogen metabolism in liver, but not in muscle (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:10868943, PubMed:17478001). In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin (PubMed:17229088). Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease (PubMed:12761548). May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions which activates KAT5/TIP60 acetyltransferase activity and promotes acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti- apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates mTORC2 complex component RICTOR at 'Thr- 1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glycogen synthase kinase 3-alpha is a multifunctional protein serine kinase. GSK-3 phosphorylates and inactivates glycogen synthase. It has also been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development. GSK-3 has been shown to regulate Cyclin D1 proteolysis and subcellular localization. GSK-3alpha (GSK-3α) regulates the production of amyloid-beta peptides, a major component of the plaques that accumulate with progression of Alzheimer's disease, by phosphorylating Tau proteins. This presents the possibility that defects in GSK-3 signaling can contribute to the onset of Alzheimer’s disease. GSK-3α can be phosphorylated by Akt at Ser21. This phosphorylation of GSK-3α negatively regulates its kinase activity.
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