c-JUN peptide comprises residues 33 - 57 of the JNK binding (δ) domain of human c-Jun. It is a JNK/c-Jun interaction inhibitor that disrupts JNK/c-Jun interaction, up-regulation of p21cip/waf and modulation of inflammatory gene expression. It Specifically induces apoptosis in HeLa tumor cells.
CAT No: R0857
CAS No:610273-01-3
Synonyms/Alias:AP-1, AP1, c-Jun, AP 1, c Jun, cJun
c-JUN peptide is a synthetic peptide fragment derived from the c-JUN protein, a key component of the activator protein-1 (AP-1) transcription factor complex. As a central regulator of gene expression, c-JUN is involved in numerous cellular processes, including proliferation, differentiation, and stress responses. The peptide sequence typically corresponds to a biologically relevant domain of the native protein, enabling researchers to probe c-JUN-mediated signaling pathways, protein-protein interactions, and transcriptional regulation in a controlled experimental context. Given its functional significance in cell signaling networks, the c-JUN peptide serves as a valuable molecular tool for dissecting the mechanistic underpinnings of AP-1 activity and related cellular events.
Signal transduction research: In cell signaling studies, the c-JUN peptide is widely used to investigate the molecular mechanisms underlying AP-1 activation and downstream gene expression. By serving as a competitive inhibitor or functional mimic of the endogenous protein, the peptide enables detailed analysis of c-JUN's role in modulating transcriptional responses to extracellular stimuli such as cytokines, growth factors, and oxidative stress. This application is particularly relevant for elucidating the dynamic regulatory networks that govern cellular adaptation and survival.
Protein interaction mapping: The peptide is frequently employed in biochemical assays to map the interaction interfaces between c-JUN and its binding partners, including other AP-1 family members and regulatory co-factors. By incorporating the peptide into pull-down experiments, surface plasmon resonance assays, or fluorescence polarization studies, researchers can quantitatively assess binding affinities, identify critical contact residues, and characterize the structural determinants of complex formation. These insights are instrumental for understanding the assembly and functional modulation of transcriptional complexes.
Kinase substrate studies: As a substrate mimic, the c-JUN peptide is utilized in kinase assays to evaluate the activity of c-JUN N-terminal kinases (JNKs) and other serine/threonine kinases that target c-JUN phosphorylation sites. By providing a defined and accessible substrate, the peptide facilitates precise measurement of kinase activity, inhibitor screening, and mechanistic studies of phosphorylation-dependent regulation. This approach supports the identification of novel modulators of kinase signaling pathways and enhances the understanding of post-translational modification dynamics.
Transcriptional regulation analysis: Researchers use the c-JUN peptide to dissect the specific contributions of c-JUN domains to transcriptional activation or repression. By introducing the peptide into cell-free transcription systems or co-transfection experiments, it is possible to selectively block or modulate the recruitment of co-activators and co-repressors, thereby clarifying the sequence-specific mechanisms that underlie AP-1-dependent gene regulation. Such studies provide valuable context for interpreting the functional consequences of c-JUN mutations and post-translational modifications in diverse biological settings.
Peptide-based inhibitor development: The c-JUN peptide serves as a foundational template for the rational design and optimization of peptide-based inhibitors targeting AP-1 signaling. By systematically modifying the peptide sequence or structure, researchers can develop analogs with enhanced binding affinity, specificity, or cellular uptake, supporting the creation of new molecular probes for functional studies. These engineered peptides are instrumental in validating potential therapeutic targets and advancing the field of transcription factor modulation in preclinical research.
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