Selective cell-permeable PKC inhibitor peptide. Consists of amino acids 19 - 31 of PKC pseudosubstrate domain linked by a disulphide bridge to a cell permeabilisation Antennapedia domain vector peptide.
CAT No: R0946
CAS No:172308-76-8
Synonyms/Alias:PKC beta pseudosubstrate;172308-76-8;PKCbetapseudosubstrate;AKOS024456784;DA-66762;PD079130;G13307;S-172308-76-8;
PKC β pseudosubstrate is a synthetic peptide inhibitor designed to mimic the autoinhibitory domain of protein kinase C beta (PKCβ). Structurally modeled after the regulatory region of PKCβ, this compound competitively binds to the substrate recognition site, thereby blocking kinase activity without undergoing phosphorylation itself. As a highly selective tool, PKC β pseudosubstrate is widely employed in signal transduction research to dissect PKCβ-mediated pathways, offering valuable insights into the regulatory mechanisms of serine/threonine kinases. Its specificity and competitive inhibition profile make it indispensable for studies aiming to elucidate the physiological and pathological roles of PKCβ in cellular processes.
Kinase inhibition studies: The peptide serves as a potent and selective inhibitor for PKCβ, enabling precise modulation of kinase activity in biochemical assays. Researchers utilize it to delineate the specific contributions of PKCβ in various phosphorylation cascades, distinguishing its effects from those of other PKC isoforms. By introducing this pseudosubstrate into in vitro kinase assays or cell lysates, scientists can assess the functional significance of PKCβ-dependent phosphorylation events and map downstream signaling networks with greater accuracy.
Signal transduction pathway analysis: PKC β pseudosubstrate is frequently used to investigate the role of PKCβ in complex signaling pathways, particularly those involved in cell growth, differentiation, and stress responses. By selectively blocking PKCβ activity, the peptide helps clarify its involvement in the regulation of diverse cellular processes such as gene expression, cytoskeletal reorganization, and vesicle trafficking. This targeted approach allows for the dissection of PKCβ-specific signaling events, facilitating the identification of novel regulatory nodes and potential intervention points.
Cellular function modulation: In cell-based experiments, the pseudosubstrate is employed to transiently inhibit PKCβ, enabling researchers to study the immediate and downstream effects of kinase suppression on cell physiology. Applications include monitoring changes in cell cycle progression, apoptosis, and metabolic regulation upon selective PKCβ inhibition. Such studies are essential for understanding the context-dependent roles of PKCβ in normal and aberrant cellular states, supporting the development of targeted research strategies.
Protein-protein interaction studies: The compound is also a valuable tool for probing the interactions between PKCβ and its binding partners. By occupying the substrate-binding site, the pseudosubstrate can disrupt or modulate the association between PKCβ and endogenous substrates or regulatory proteins. This property is leveraged in co-immunoprecipitation assays and other biochemical techniques to unravel the molecular determinants of PKCβ substrate specificity and interaction dynamics.
Peptide inhibitor validation: As a well-characterized synthetic peptide, PKC β pseudosubstrate is routinely applied in the validation of novel assay systems designed to screen for kinase inhibitors or to characterize the selectivity of potential drug candidates. Its defined mechanism of action and established inhibitory profile provide a reliable benchmark for assay calibration, quality control, and comparative analysis in high-throughput screening or mechanistic enzymology studies. By serving as a reference standard, the peptide enhances the rigor and reproducibility of kinase research workflows.
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