c-Myc Peptide Trifluoroacetate is a synthetic peptide corresponding to the C-terminal amino acids (410-419) of human c-myc protein, and participates in regulation of growth-related gene transcription.
CAT No: R1294
c-Myc Peptide Trifluoroacetate is a synthetic peptide fragment corresponding to a specific epitope within the c-Myc protein, a well-characterized transcription factor implicated in cell cycle regulation, proliferation, and oncogenic transformation. As a chemically defined peptide supplied as its trifluoroacetate salt, it is widely utilized in molecular and cellular biology research, particularly in studies involving protein-protein interactions, antibody validation, and signal transduction pathways. The sequence of this peptide is designed to mimic a region of the human c-Myc protein, enabling its use as a standard or probe in a variety of biochemical assays. Its relevance is underscored by the central role of c-Myc in gene regulation and its frequent dysregulation in cancer biology, making this peptide a valuable tool for dissecting molecular mechanisms and supporting experimental reproducibility.
Epitope mapping: The c-Myc peptide serves as a critical reagent for mapping antibody specificity and affinity in immunological assays. By providing a defined linear epitope, it enables researchers to characterize monoclonal and polyclonal antibodies directed against c-Myc, facilitating the development and validation of immunodetection techniques such as Western blotting, enzyme-linked immunosorbent assays (ELISA), and immunoprecipitation. Its use in epitope mapping helps ensure that antibodies selectively recognize the intended sequence, minimizing cross-reactivity and enhancing assay reliability.
Protein interaction studies: As a molecular mimic of a functional domain within the c-Myc protein, this peptide is frequently employed to investigate protein-protein interactions involving c-Myc and its binding partners. By serving as a competitive inhibitor or affinity probe, it allows researchers to dissect the molecular determinants of c-Myc association with regulatory proteins, transcriptional co-factors, or DNA-binding complexes. Such studies provide insight into the mechanisms underlying c-Myc-mediated gene regulation and contribute to a deeper understanding of cellular signaling pathways.
Peptide competition assays: In functional assays, the c-Myc peptide is used to competitively inhibit endogenous c-Myc interactions, enabling the assessment of binding specificity and the functional importance of the targeted epitope. By introducing the peptide into in vitro or cellular systems, researchers can probe the contribution of c-Myc to various signaling cascades, transcriptional events, or protein assemblies. These competition experiments are instrumental in elucidating the biological roles of c-Myc and validating the specificity of experimental reagents.
Immunoassay standards: The defined sequence and chemical uniformity of this peptide make it an ideal standard for quantitative and qualitative immunoassays. It can be used to calibrate assay sensitivity, establish detection thresholds, or serve as a positive control in antibody-based detection systems. Incorporating the peptide into assay protocols enhances reproducibility and data comparability across experiments, supporting robust and reliable measurement of c-Myc-related signals.
Peptide synthesis and modification studies: Beyond its role as a functional probe, the c-Myc peptide trifluoroacetate is valuable in peptide chemistry research, including studies on peptide synthesis, purification, and post-synthetic modifications. Its well-characterized sequence serves as a model substrate for optimizing solid-phase synthesis protocols or for evaluating the effects of chemical modifications such as labeling, cyclization, or conjugation. These applications advance the development of novel peptide-based tools and methodologies for biochemical research.
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