Stearated form of peptide Ht-31; Cell-permeable inhibitor of the interaction between the RII subunits of cAMP-dependent PKA and A-kinase anchoring protein (AKAP) in cell extracts.
CAT No: R1080
CAS No:188425-80-1
Synonyms/Alias:st-Ht31;188425-80-1;CID 16143012;L-Tyrosine,N-(1-oxooctadecyl)-L-a-aspartyl-L-leucyl-L-isoleucyl-L-a-glutamyl-L-a-glutamyl-L-alanyl-L-alanyl-L-seryl-L-arginyl-L-isoleucyl-L-valyl-L-a-aspartyl-L-alanyl-L-valyl-L-isoleucyl-L-a-glutamyl-L-glutaminyl-L-valyl-L-lysyl-L-alanyl-L-alanylglycyl-L-alanyl-;AKOS032962858;DA-58113;PD080160;stearoyl-Asp-Leu-Ile-Glu-Glu-Ala-Ala-Ser-Arg-Ile-Val-Asp-Ala-Val-Ile-Glu-Gln-Val-Lys-Ala-Ala-Gly-Ala-Tyr-OH;
st-Ht31 is a synthetic peptide widely recognized for its role as a competitive inhibitor of A-kinase anchoring protein (AKAP) interactions with protein kinase A (PKA). Structurally designed to mimic the amphipathic helix region of AKAPs, st-Ht31 disrupts the spatial organization of PKA by preventing its anchoring to cellular scaffolds. This property makes the peptide a valuable molecular tool for dissecting compartmentalized cAMP signaling pathways and elucidating the functional significance of AKAP-mediated PKA localization in diverse biological processes. Its application extends across molecular signaling research, cell biology, and biochemistry, where precise modulation of PKA activity is essential for understanding intracellular signaling dynamics.
Signal transduction studies: As a potent disruptor of AKAP-PKA interactions, st-Ht31 is extensively employed to investigate the spatial regulation of cAMP-dependent signaling cascades. By selectively dissociating PKA from its anchoring proteins, researchers can delineate the effects of localized versus global PKA activity on downstream targets. This targeted approach enables a deeper understanding of how compartmentalization influences signal specificity, duration, and amplitude within various cellular contexts, including neuronal, cardiac, and endocrine systems.
Cellular compartmentalization research: The peptide serves as a critical tool for probing the functional consequences of PKA delocalization within cells. Utilizing st-Ht31, scientists can experimentally disrupt the microdomain-specific actions of PKA, thereby revealing the physiological importance of discrete signaling pools. Such studies are instrumental in mapping the spatial organization of kinase activity, identifying novel anchoring complexes, and elucidating the molecular basis of compartmentalized signaling networks that govern cell growth, differentiation, and metabolic regulation.
Phosphorylation pathway analysis: In biochemical assays, st-Ht31 is applied to modulate phosphorylation events mediated by PKA in vitro and in cell-based systems. By preventing the association of PKA with AKAPs, the peptide allows for the assessment of phosphorylation patterns that are dependent on precise subcellular localization. This application is particularly valuable for distinguishing direct substrate phosphorylation by free versus anchored PKA, thereby enhancing the specificity and interpretability of kinase-substrate relationship studies.
Drug discovery and screening: The unique ability of st-Ht31 to disrupt protein-protein interactions between AKAPs and PKA positions it as an important reagent in high-throughput screening platforms. Researchers leverage the peptide to identify novel modulators of AKAP-PKA binding or to validate the functional relevance of candidate compounds targeting this interface. Its use in these assays supports the identification of small molecules or peptides with potential as research tools or as leads for further development in the context of intracellular signaling modulation.
Functional genomics and proteomics: In systems biology approaches, st-Ht31 is integrated into experimental workflows to explore the broader impact of AKAP-mediated signaling on gene expression and protein networks. By perturbing anchoring interactions, investigators can assess changes in transcriptional profiles, protein phosphorylation states, and interaction networks, providing insights into the global regulatory mechanisms orchestrated by localized kinase activity. These applications support the elucidation of complex signaling architectures and facilitate the discovery of novel regulatory nodes within the cAMP/PKA axis.
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