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G4296

Sigma-Aldrich

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

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

200

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.

P49841

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

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

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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EU REACH Annex XVII (Restriction List)

CAS No.

Vyberte jednu z posledních verzí:

Osvědčení o analýze (COA)

Lot/Batch Number
SLCL5362
SLCK0497
SLCH0070
SLBZ6891
SLBV5295

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Glycogen synthase kinase 3 in Wnt signaling pathway and cancer
Nydia Tejeda-Mu?oz
IUBMB Life (2015)
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
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
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.
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