PKA Inhibitor peptide, The PKA Inhibitor peptide controls the biological activity of PKA. This small molecule/inhibitor is primarily used for Neuroscience applications.
Routinely evaluated by inhibition of PKA catalytic subunit (14-114).
Forme physique
Lyophilized powder (from H2O)
Stockage et stabilité
Lyophilized: Stable for 2 years at -20°C . Rehydrated: Stable for 1 year at -20°C.
Informations légales
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Clause de non-responsabilité
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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The Journal of biological chemistry, 276(20), 16969-16977 (2001-03-30)
The hepatitis B virus-X (HBx) protein is known as a multifunctional protein that not only coactivates transcription of viral and cellular genes but coordinates the balance between proliferation and programmed cell death, by inducing or blocking apoptosis. In this study
The Journal of biological chemistry, 272(8), 4970-4977 (1997-02-21)
We have previously reported that phosphorylation of adenylyl cyclase type VI (AC6) may result in the suppression of adenylyl cyclase activity during desensitization of the A2a-adenosine receptor-mediated cAMP response (A2a desensitization) in rat pheochromocytoma PC12 cells. In the present study
Primary structural determinants essential for potent inhibition of cAMP-dependent protein kinase by inhibitory peptides corresponding to the active portion of the heat-stable inhibitor protein.
Glass, D B, et al.
The Journal of Biological Chemistry, 264, 8802-8810 (1989)
Protein kinases are enzymes whose abundance, protein-protein interactions, and posttranslational modifications together determine net signaling activity in cells. Large-scale data on cellular kinase activity are limited, because existing assays are cumbersome, poorly sensitive, low throughput, and restricted to measuring one
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