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AB42597

Recombinant human GSK3 alpha protein (GST tag N-Terminus)

Recombinant human GSK3 alpha protein (GST tag N-Terminus)

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(3 Publications)

Recombinant human GSK3 alpha protein (GST tag N-Terminus) is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for FuncS.

別名を表示する

Glycogen synthase kinase-3 alpha, GSK-3 alpha, Serine/threonine-protein kinase GSK3A, GSK3A

Key facts

精製度

>80% SDS-PAGE

発現系

Baculovirus infected Sf9 cells

タグ

GST tag N-Terminus

アプリケーション

FuncS

applications

生物活性

Yes

生物学的活性

700 U/mg. One unit is defined as the amount of enzyme that will phosphorylate 1 nmol of glycogen synthase peptide 2 substrate per minute at pH 7.4 and 30C. Assay buffer: 50 mM HEPES, pH 7.4, 3 mM MgCl2, 3 mM MnCl2, 1 mM DTT, 3uM Na-orthovanadate, 0.1 mM ATP, 20 uM substrate, and 0.1 ug recombinant GSK3 alpha.

アクセッション番号

P49840

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.307% Glutathione, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.</p>" } } }

製品の詳細

Expressed in a Baculovirus infected Sf9 cell expression system.

配列情報

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P49840","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
True

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Glycogen synthase kinase 3 alpha (GSK3 alpha) is a serine/threonine protein kinase also known as GSK3A with a molecular mass of approximately 51 kDa. It plays an important role in the regulation of various cellular processes. GSK3 alpha is expressed in many tissues but has high levels in the brain heart and skeletal muscle. It participates in the phosphorylation of numerous substrates impacting their activity and stability.
Biological function summary

GSK3 alpha influences several cellular functions including cell division differentiation and apoptosis. It functions independently or as part of a protein complex often forming dimeric complexes with GSK3 beta. GSK3 alpha alters the activity of numerous transcription factors and regulates insulin and Wnt signaling pathways affecting glucose metabolism and cellular growth.

Pathways

GSK3 alpha is involved in the Wnt and insulin signaling pathways. In the Wnt pathway GSK3 alpha phosphorylates beta-catenin marking it for degradation and controlling gene expression. In the insulin pathway it modulates glycogen synthesis and affects glucose homeostasis. GSK3 alpha interacts closely with proteins like APC and glycogen synthase making it integral to these pathways.

GSK3 alpha links to neurodegenerative disorders and diabetes. Its dysfunction contributes to Alzheimer’s disease where abnormal phosphorylation of tau protein occurs. In the context of diabetes GSK3 alpha influences glucose regulation impacting insulin sensitivity and action. The interplay between GSK3 alpha and tau in Alzheimer's as well as insulin signaling proteins illustrates its important role in these disease pathways.

製品の性状

製品の状態

Liquid

補足情報

Affinity purified.

一般的な情報

機能

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).

配列の類似性

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.

翻訳後修飾

Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279.. (Microbial infection) Dephosphorylated at Tyr-279 by M.tuberculosis PtpA, which leads to prevention of apoptosis during early stages of microbial infection.

製品プロトコール

ターゲットの情報

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).
See full target information Glycogen synthase kinase-3 alpha

文献 (3)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 12:2346 PubMed33879767

2021

ARIH1 signaling promotes anti-tumor immunity by targeting PD-L1 for proteasomal degradation.

Applications

Unspecified application

Species

Unspecified reactive species

Youqian Wu,Chao Zhang,Xiaolan Liu,Zhengfu He,Bing Shan,Qingxin Zeng,Qingwei Zhao,Huaying Zhu,Hongwei Liao,Xufeng Cen,Xiaoyan Xu,Mengmeng Zhang,Tingjun Hou,Zhe Wang,Huanhuan Yan,Shuying Yang,Yaqin Sun,Yanying Chen,Ronghai Wu,Tingxue Xie,Wei Chen,Ayaz Najafov,Songmin Ying,Hongguang Xia

International journal of molecular sciences 21: PubMed33218072

2020

Discovery and Design of Novel Small Molecule GSK-3 Inhibitors Targeting the Substrate Binding Site.

Applications

Unspecified application

Species

Unspecified reactive species

Ido Rippin,Netaly Khazanov, Shirley Ben Joseph,Tania Kudinov,Eva Berent,Sara Melisa Arciniegas Ruiz,Daniele Marciano,Laura Levy,Arie Gruzman,Hanoch Senderowitz,Hagit Eldar-Finkelman

The Journal of biological chemistry 293:14798-14811 PubMed30072381

2018

The Ras-like GTPase Rem2 is a potent inhibitor of calcium/calmodulin-dependent kinase II activity.

Applications

Unspecified application

Species

Unspecified reactive species

Leandro Royer,Josiah J Herzog,Katelyn Kenny,Boriana Tzvetkova,Jesse C Cochrane,Michael T Marr,Suzanne Paradis
View all publications

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