Protein Kinase C (19-31), a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate peptide for testing the protein kinase C activity. Protein kinase C (PKC) is involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins.
CAT No: R1639
CAS No:121545-65-1
Synonyms/Alias:Protein Kinase C (19-31);121545-65-1;PKC (19-31);Pseudosubstrate;DA-57155;
Protein Kinase C 19-31 is a synthetic peptide fragment corresponding to amino acids 19 through 31 of the Protein Kinase C (PKC) enzyme. As a representative segment of the regulatory domain of PKC, this peptide is widely utilized in biochemical and cellular research to elucidate the structure-function relationships within the PKC family. PKC enzymes are serine/threonine kinases pivotal to signal transduction pathways that govern a range of cellular processes, including proliferation, differentiation, and gene expression. The PKC 19-31 peptide serves as a valuable molecular tool for dissecting the mechanisms of PKC activation, substrate recognition, and protein-protein interactions, offering researchers a focused approach to study this critical kinase's regulatory elements.
Signal transduction studies: Researchers frequently employ the PKC 19-31 peptide to investigate the intricate signaling cascades mediated by PKC isoforms. By mimicking the native sequence within the regulatory domain, this peptide can be used to probe the binding affinities of regulatory proteins, lipids, and cofactors that modulate PKC activity. Such studies deepen understanding of how PKC responds to second messengers like diacylglycerol and calcium, providing insight into the spatial and temporal regulation of kinase activity within cellular contexts.
Protein-protein interaction assays: The PKC 19-31 fragment is instrumental in mapping interaction sites between PKC and its regulatory partners. In vitro binding assays and pull-down experiments utilize this peptide to identify and characterize proteins that interact with the regulatory domain. These applications help delineate the molecular determinants of PKC complex formation and facilitate the discovery of novel modulators or scaffolding proteins that influence kinase localization and function.
Peptide inhibitor development: As a sequence-specific mimic of a regulatory region, the PKC 19-31 peptide can serve as a lead structure in the design of peptide-based inhibitors. By competing with endogenous sequences for binding to PKC or its interacting partners, it enables the assessment of inhibitory potential and specificity. This approach is valuable in structure-activity relationship studies aimed at understanding how targeted peptides can modulate kinase function, which is essential for the rational development of research tools for pathway dissection.
Phosphorylation studies: The defined sequence of the PKC 19-31 peptide makes it a suitable substrate or competitor in kinase assays designed to examine phosphorylation events. Researchers can utilize it to monitor site-specific phosphorylation by PKC or related kinases, facilitating the elucidation of substrate preferences and catalytic mechanisms. This application supports the exploration of phosphorylation-dependent signaling networks and the identification of consensus motifs within kinase substrates.
Structural and conformational analysis: The use of the PKC 19-31 peptide extends to structural biology, where it aids in elucidating the conformational dynamics of the regulatory domain. Techniques such as NMR spectroscopy and circular dichroism can be applied to study the secondary structure and folding properties of the peptide in solution. These structural insights contribute to a more comprehensive understanding of PKC regulation at the molecular level and inform the design of further experimental probes or modulators based on the regulatory domain architecture.
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