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
UNSPSC Code:
12352200
NACRES:
NA.32
Productos recomendados
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
143-193 nmol/min·mg
mol wt
~48 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... GSK3B(2932)
General description
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.
Biochem/physiol Actions
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).
Physical form
Supplied in 50mM NaPhosphate pH 7.0, 300 mM NaCl, 150 mM imidazole, 0.1mM PMSF, 0.2 mM DTT, 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Faceshields, Gloves, Goggles, type ABEK (EN14387) respirator filter
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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.
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
Glycogen synthase kinase 3 in Wnt signaling pathway and cancer
Nydia Tejeda-Mu?oz
IUBMB Life (2015)
Richard S Jope et al.
Trends in biochemical sciences, 29(2), 95-102 (2004-04-23)
Glycogen synthase kinase-3 (GSK3) is now recognized as a key component of a surprisingly large number of cellular processes and diseases. Several mechanisms play a part in controlling the actions of GSK3, including phosphorylation, protein complex formation, and subcellular distribution.
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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