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Sigma-Aldrich

GSM (GSK3 substrate peptide)

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eCl@ss:
32160405
NACRES:
NA.41

mol wt

Mw 2673 Da

Quality Level

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable (kinase)

NCBI accession no.

UniProt accession no.

shipped in

dry ice

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12-34012-37312-152
Sigma-Aldrich

Sigma-Aldrich

12-152

PKA Substrate Peptide

technique(s)

activity assay: suitable (kinase)

technique(s)

activity assay: suitable (kinase)

technique(s)

activity assay: suitable (kinase)

technique(s)

activity assay: suitable (kinase)

UniProt accession no.

P49840

UniProt accession no.

P31749

UniProt accession no.

O14757, O96017

UniProt accession no.

P17612

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

shipped in

wet ice

Quality Level

100

Quality Level

100

Quality Level

300

Quality Level

100

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

Application

GSM (GSK3 substrate peptide) has been used:
  • in in vitro glycogen synthase kinase 3 (GSK-3)-3β activity assay to measure the kinase activity of GSK-3
  • as a supplement in perfusates in kinase activity assay to determine the effect of the phosphatase-activating domain (PAD) peptide on squid axoplasm
  • as a control in Kinase-Glo luminescent kinase assay to measure the influence of ibuprofen treatment on the catalytic activity of the kinase GSK3β

Biochem/physiol Actions

Glycogen synthase kinase 3 (GSK3) is a protein kinase, which regulates glycogen metabolism. It regulates various cell functions, like signaling by insulin, growth factors and nutrients, and the specification of cell fates during embryonic development. GSK3 is involved modulating in apoptosis, cell division, and microtubule function.

Quality

Routinely evaluated as a substrate for GSK3β (Catalog # 14-306).

Physical form

1 mg of GSM lyophilized from 1 mL sterile, distilled water. Lyophilized powder.

Storage and Stability

Lyophilized: 2 years at -20°C. Rehydrated: 6 months at -20°C

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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P Cohen et al.
Nature reviews. Molecular cell biology, 2(10), 769-776 (2001-10-05)
Glycogen synthase kinase 3 (GSK3) was initially described as a key enzyme involved in glycogen metabolism, but is now known to regulate a diverse array of cell functions. The study of the substrate specificity and regulation of GSK3 activity has
Vânia Gonçalves et al.
Oncotarget, 11(47), 4421-4437 (2020-12-15)
A major risk factor promoting tumor development is chronic inflammation and the use of nonsteroidal anti-inflammatory drugs (NSAID), including ibuprofen, can decrease the risk of developing various types of cancer, including colorectal cancer (CRC). Although the molecular mechanism behind the
An assay for glycogen synthase kinase 3 (GSK-3) for use in crude cell extracts
Ryves, W. J., et al
Analytical biochemistry, 264, 124-127 (1998)
Nydia Tejeda-Muñoz et al.
Molecular and cellular biology, 36(5), 731-741 (2015-12-30)
The molecular events that drive Wnt-induced regulation of glycogen synthase kinase 3β (GSK-3β) activity are poorly defined. In this study, we found that protein kinase Cζ (PKCζ) and GSK-3β interact mainly in colon cancer cells. Wnt stimulation induced a rapid
Nicholas M Kanaan et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 31(27), 9858-9868 (2011-07-08)
Aggregated filamentous forms of hyperphosphorylated tau (a microtubule-associated protein) represent pathological hallmarks of Alzheimer's disease (AD) and other tauopathies. While axonal transport dysfunction is thought to represent a primary pathogenic factor in AD and other neurodegenerative diseases, the direct molecular

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