12-340
Akt/SGK Substrate Peptide
Akt/SGK Substrate Peptide primarily used in Kinase Assays.
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About This Item
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Quality Level
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
NCBI accession no.
UniProt accession no.
shipped in
dry ice
Biochem/physiol Actions
Protein Target: Akt
Target Sub-Family: AGC
Quality
Routinely evaluated by Kinase Assay as a substrate for Akt1/PKB and SGK active enzymes.
Physical form
sterile deionized water
Storage and Stability
2 years 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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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The Journal of biological chemistry, 276(11), 8516-8523 (2000-12-16)
CAAT/enhancer-binding proteins (C/EBPs) play an important role in the regulation of gene expression in insulin-responsive tissues. We have found that a complex containing C/EBPbeta interacts with an insulin response sequence in the insulin-like growth factor-binding protein-1 (IGFBP-1) gene and that
FEBS letters, 399(3), 333-338 (1996-12-16)
The substrate specificity of protein kinase-B alpha (PKBalpha, also known as RAC kinase or Akt) was investigated using synthetic peptide substrates related to the sequence surrounding the phosphorylation site on glycogen synthase kinase-3 (GSK3). The minimum sequence motif required for
The Journal of biological chemistry, 276(35), 33213-33219 (2001-07-07)
N-terminal tail phosphorylation of histone H3 plays an important role in gene expression, chromatin remodeling, and chromosome condensation. Phosphorylation of histone H3 at serine 10 was shown to be mediated by RSK2, mitogen- and stress-activated protein kinase-1 (MSK1), and mitogen-activated
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