G4296
GSK3β, active, His tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Produit recombinant
expressed in baculovirus infected Sf9 cells
Niveau de qualité
Gamme de produits
PRECISIO® Kinase
Pureté
≥70% (SDS-PAGE)
Forme
buffered aqueous glycerol solution
Activité spécifique
143-193 nmol/min·mg
Poids mol.
~48 kDa
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... GSK3B(2932)
Description générale
Research area: Cellsignalling. GSK3B (glycogen synthase kinase 3β) is one of the two isoforms of GSK3 enzyme, both of which are encoded by different genes. This protein is predominantly cytoplasmic, but is also found to be localized to nucleus and mitochondria. It is a protein-serine kinase. This protein contains a protein kinase domain in its core, and is composed of 482 amino acids with a molecular weight of 46,712Da. It shows a wide range of tissue expression with the highest expression in brain.
Application
GSK3β, active, His tagged human has been used as an incubating medium during in vitro hyperphosphorylation of tau protein.
Actions biochimiques/physiologiques
GSK3β is a serine-threonine protein kinase that was originally identified as the kinase that phosphorylates and inhibits glycogen synthase.GSK3β is ubiquitously present in human tissues and implicated in the regulation of several physiological processes, including the control of glycogen and protein synthesis by insulin and modulation of the transcription factors AP-1 and CREB. Transient transfection of human GSK3β into Chinese hamster ovary cells stably transfected with individual human tau isoforms leads to hyperphosphorylation of tau at all the sites investigated with phosphorylation-dependent anti-tau antibodies.
Glycogen Synthase Kinase 3β (GSK3β) is responsible for rapid cyclin D1 turnover by phosphorylating it on Thr-286. It functions as a negative regulator of Wnt signaling during embryonic development and cell proliferation in adult tissues. This protein phosphorylates and regulates multiple proteins, such as glycogen synthase, insulin receptor substrate-1, axin and APC (adenomatous polyposis coli). This protein is also shown to interact with multiple proteins which are linked with Alzheimer′s disease (AD).
Forme physique
Supplied in 50mM NaPhosphate pH 7.0, 300 mM NaCl, 150 mM imidazole, 0.1mM PMSF, 0.2 mM DTT, 25% glycerol.
Informations légales
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Code de la classe de stockage
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Faceshields, Gloves, Goggles, type ABEK (EN14387) respirator filter
Certificats d'analyse (COA)
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Glycogen synthase kinase 3 in Wnt signaling pathway and cancer
Nydia Tejeda-Mu?oz
IUBMB Life (2015)
Lannah S Abasi et al.
Communications biology, 7(1), 251-251 (2024-03-02)
Tau is a microtubule-associated protein often found in neurofibrillary tangles (NFTs) in the brains of patients with Alzheimer's disease. Beyond this context, mounting evidence suggests that tau localizes into the nucleus, where it may play a role in DNA protection
C Sutherland et al.
The Biochemical journal, 296 ( Pt 1), 15-19 (1993-11-15)
The beta-isoform of glycogen synthase kinase-3 (GSK3 beta) isolated from rabbit skeletal muscle was inactivated 90-95% following incubation with MgATP and either MAP kinase-activated protein kinase-1 (MAPKAP kinase-1, also termed RSK-2) or p70 S6 kinase (p70S6K), and re-activated with protein
B R Sperber et al.
Neuroscience letters, 197(2), 149-153 (1995-09-08)
Hyperphosphorylated tau protein is the major constituent of the paired helical filament (PHF), the major fibrous component of the neurofibrillary lesions of Alzheimer's disease (AD). Hyperphosphorylation of tau is believed to be the critical event that leads to filament assembly.
Bettina M Foidl et al.
Frontiers in aging neuroscience, 10, 113-113 (2018-05-05)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder of the brain, characterized by extracellular aggregation of beta-amyloid (Aβ) and hyperphosphorylation of tau causing intraneuronal neurofibrillary tangles (NFTs). There is urgent need to study the interactions between Aβ and tau, especially
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