PKA inhibitor fragment (6-22) amide is the shortest synthetic PKI peptide, and acts as a potent protein kinase A (PKA) inhibitor.
CAT No: R0953
CAS No:121932-06-7
Synonyms/Alias:121932-06-7;L-Isoleucinamide, L-threonyl-L-tyrosyl-L-alanyl-L-alpha-aspartyl-L-phenylalanyl-L-isoleucyl-L-alanyl-L-serylglycyl-L-arginyl-L-threonylglycyl-L-arginyl-L-arginyl-L-asparaginyl-L-alanyl-;Tyadfiasgrtgrrnai-nh2;MFCD00133792;HB0508;AKOS024456843;C80H130N28O24;DA-76934;FP111129;PKA Inhibitor (6-22) amide trifluoroacetate salt;PKA Inhibitor 6-22 Amide - CAS 121932-06-7;H-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH2; H-TYADFIASGRTGRRNAI-NH2;
PKA inhibitor fragment (6-22) amide is a synthetic peptide derived from the protein kinase A (PKA) regulatory subunit, specifically encompassing amino acid residues 6 through 22 in an amidated form. As a well-characterized peptide inhibitor, it is widely utilized to selectively block the activity of PKA, a pivotal serine/threonine kinase involved in numerous cellular signaling pathways mediated by cyclic adenosine monophosphate (cAMP). The capacity of this fragment to competitively inhibit PKA's catalytic subunit underpins its value as a molecular tool for dissecting cAMP-dependent signaling mechanisms in a broad spectrum of biochemical and cell biology research contexts.
Signal Transduction Studies: The peptide fragment serves as a highly specific probe for investigating cAMP-dependent signaling cascades. By selectively inhibiting PKA activity, researchers can delineate the direct contributions of PKA-mediated phosphorylation events within complex cellular networks. This approach enables the functional dissection of downstream effectors and regulatory nodes modulated by cAMP in processes such as gene expression, metabolism, and ion channel regulation, providing clarity on the precise role of PKA in diverse cellular models.
Kinase Assay Development: In biochemical assays designed to measure kinase activity, the PKA inhibitor fragment is routinely employed as a reference or control to validate assay specificity. Its ability to selectively inhibit PKA, without affecting other kinases, allows for the establishment of reliable negative controls and the quantification of basal versus stimulated phosphorylation events. This application is particularly valuable in high-throughput screening platforms that require stringent validation of target engagement and pathway selectivity.
Peptide-Protein Interaction Analysis: The fragment's defined sequence and inhibitory properties make it a powerful tool for studying protein-protein interactions involving PKA and its substrates or regulatory partners. By competitively binding to the catalytic subunit, the inhibitor peptide can be used to map substrate recognition motifs and to assess the structural determinants of kinase-substrate specificity. Such studies are critical for understanding the molecular basis of signal fidelity and for the rational design of novel modulators targeting PKA-related pathways.
Cellular Functional Studies: In cellular and ex vivo systems, the inhibitor fragment is frequently utilized to transiently suppress PKA activity and observe resultant phenotypic changes. This approach facilitates the investigation of PKA's role in cellular proliferation, differentiation, apoptosis, and other physiological processes. The reversible and selective nature of the peptide's inhibition enables precise temporal control, supporting mechanistic studies that require acute modulation of kinase function without long-term genetic manipulation.
Peptide Inhibitor Validation: The PKA inhibitor fragment is also instrumental in benchmarking the efficacy of newly developed peptide or small-molecule inhibitors targeting PKA. By serving as a reference standard, it allows for the comparative evaluation of inhibitor potency, selectivity, and mechanism of action in both in vitro and cell-based assays. This application is essential for drug discovery workflows and for advancing the development of next-generation modulators of PKA signaling.
Collectively, the multifaceted applications of the PKA inhibitor fragment (6-22) amide underscore its importance as a precision tool in the study of kinase signaling, peptide-protein interactions, and the broader landscape of cAMP-mediated regulatory mechanisms. Its use enhances experimental rigor and interpretability in both fundamental and applied biochemical research.
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