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Using InCELLect™ Cell-Permeable,
Stearated Peptides to Probe cAMP-Dependent Protein Kinase-Mediated Cellular Signaling
Reactions In Vivo
Said Goueli, Ph.D., and Kevin Hsiao, M.S.
Promega Corporation
Protein kinase- and phosphatase-mediated phosphorylation and dephosphorylation are key
mechanisms used in cellular regulation. In addition to activation, precise subcellular
localization is required for signaling specificity in response to a stimulus.
Protein-protein interaction facilitates appropriate associations among members of a
signaling cascade, which can be in the form of a scaffold or an anchor. Peptides derived
from anchoring proteins can disrupt the interaction between enzymes and their
anchoring proteins. A peptide derived from the A Kinase-Anchoring Protein (AKAP) Ht-31
(human thyroid) disrupts A kinase anchoring and thus A kinase-mediated responses in
several model systems.
We have generated stearated forms of the peptide, InCELLect™ AKAP St-Ht31
(Cat,# V8211), and its corresponding control peptide, InCELLect™ St-Ht31P
(Cat.# V8221), which are cell permeable and facilitate the study of AKAP in mediating PKA
responses. This article describes recent research using Promega's stearated
peptides-InCELLect™ AKAP St-Ht31 Inhibitor Peptide and InCELLect™
St-Ht31P Control Peptide--on PKA anchoring in the cell.
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