c-Myc Peptide mimics a key transactivation domain of the c-Myc protein involved in PPI interactions. Acidic, aromatic, and hydrophobic residues contribute to structural adaptability. Researchers study its binding to transcriptional coactivators and dynamic structural features. Applications include PPI analysis, transcription-factor modeling, and inhibitor design.
CAT No: R2390
CAS No:145646-22-6
Synonyms/Alias:c-Myc Peptide;145646-22-6;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-5-amino-2-[[(2S)-2-amino-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]-4-methylpentanoic acid;G90894;
c-Myc Peptide is a synthetic peptide corresponding to a specific amino acid sequence derived from the human c-Myc oncoprotein, a transcription factor that plays a pivotal role in cell cycle progression, apoptosis, and cellular transformation. As a key regulator of gene expression, c-Myc is extensively studied in the context of cancer biology, cell proliferation, and signal transduction pathways. The peptide is widely utilized in biochemical and molecular research as a tool for investigating protein-protein interactions, antibody recognition, and functional characterization of c-Myc-related mechanisms. Its defined sequence and structural features make it an invaluable reagent for probing the biological activities and regulatory networks associated with the c-Myc protein.
Epitope mapping and antibody validation: Researchers frequently employ the c-Myc peptide as a standard for epitope mapping and antibody specificity testing. By providing a well-characterized antigenic determinant, the peptide enables precise evaluation of monoclonal and polyclonal antibodies that target the c-Myc tag or endogenous c-Myc protein. This application is essential for ensuring the reliability of immunodetection assays such as Western blotting, immunoprecipitation, immunofluorescence, and enzyme-linked immunosorbent assays. The peptide's defined sequence allows for rigorous assessment of antibody cross-reactivity and binding affinity, supporting the development and validation of high-quality immunological reagents.
Protein-protein interaction studies: The c-Myc peptide serves as a model substrate for dissecting the molecular interactions between c-Myc and its binding partners. By mimicking the functional domain of the native protein, the peptide facilitates in vitro assays aimed at characterizing the specificity, kinetics, and structural determinants of c-Myc-mediated complexes. Applications include competitive binding assays, affinity chromatography, and structural analyses using techniques such as NMR spectroscopy or X-ray crystallography. These studies advance understanding of c-Myc's role in transcriptional regulation and its involvement in oncogenic signaling pathways.
Peptide-based assay development: The defined sequence and biochemical properties of the c-Myc peptide make it an ideal component in the design of peptide-based assays for high-throughput screening and quantitative analysis. It is commonly incorporated into ELISA formats, competitive binding assays, and fluorescence polarization assays to enable sensitive detection of c-Myc interactions or inhibitors. Such assays are instrumental in drug discovery efforts targeting the c-Myc pathway, as well as in the quantitative assessment of c-Myc activity in cellular extracts or recombinant systems.
Affinity purification of tagged proteins: In recombinant protein expression systems, the c-Myc epitope is frequently engineered as a fusion tag to facilitate detection and purification. The synthetic peptide can be used as a competitive elution agent or as a ligand immobilized on chromatography matrices for the selective isolation of c-Myc-tagged proteins. This approach streamlines the purification workflow, enhances yield and purity, and preserves the functional integrity of the target protein. The use of the peptide in affinity purification protocols is particularly valuable in proteomics, structural biology, and functional studies requiring high-quality recombinant proteins.
Signal transduction and functional analysis: Utilizing the c-Myc peptide in cellular and biochemical assays provides a controlled system for investigating the downstream effects of c-Myc activation or inhibition. By serving as a competitive inhibitor or molecular probe, the peptide enables researchers to dissect signaling cascades, transcriptional networks, and post-translational modifications associated with c-Myc function. These studies contribute to elucidating the regulatory mechanisms governing cell proliferation, differentiation, and transformation, offering insight into the broader implications of c-Myc dysregulation in disease and development.
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