p53 (139-147)

p53 (139-147) is a synthetic peptide fragment corresponding to amino acid residues 139 through 147 of the human tumor suppressor protein p53. As a defined segment of a critical regulatory protein, this peptide serves as a valuable molecular tool for researchers investigating the structural and functional aspects of p53, which is central to cellular responses such as DNA repair, cell cycle control, and apoptosis. The sequence encompasses a region implicated in protein-protein interactions, making it particularly relevant for studies focused on the mechanistic underpinnings of p53's biological roles. Owing to its precise composition and well-characterized origin, the peptide is widely utilized in biochemical, structural, and cellular research contexts that aim to elucidate the pathways governed by p53 and its interaction partners.

Protein-protein interaction studies: The 139-147 peptide segment is frequently employed in assays designed to characterize the interaction surfaces between p53 and its binding partners. By providing a discrete epitope, the peptide enables detailed mapping of contact points involved in molecular recognition, particularly for proteins such as MDM2 or other regulatory elements that modulate p53 stability and activity. Researchers utilize this peptide in binding assays, surface plasmon resonance, and co-immunoprecipitation experiments to dissect the molecular determinants of these interactions, thereby advancing the understanding of regulatory networks involving p53.

Epitope mapping and antibody validation: As a defined linear epitope, the peptide is instrumental in the development and validation of antibodies targeting p53. It is used to assess antibody specificity and affinity in enzyme-linked immunosorbent assays (ELISA), Western blotting, and immunoprecipitation protocols. By serving as a positive control or competitive inhibitor, the peptide facilitates the identification of antibodies that recognize the 139-147 region, supporting the generation of reliable reagents for downstream applications in p53 research.

Peptide-based inhibitor screening: The 139-147 sequence can be incorporated into screening platforms aimed at discovering small molecules or peptides that disrupt p53 interactions with its negative regulators. By mimicking a critical binding motif, the peptide is used in high-throughput assays to evaluate the efficacy of candidate compounds in modulating p53 activity. Such studies are essential for the identification of novel chemical probes or research leads that target the regulatory axis of p53, offering insights into mechanisms of protein inhibition and stabilization.

Structural biology and conformational analysis: The defined nature of the 139-147 peptide makes it suitable for structural investigations using techniques such as nuclear magnetic resonance (NMR) spectroscopy or X-ray crystallography. Researchers utilize the peptide to obtain high-resolution information on the conformation of this p53 segment, both in isolation and in complex with interacting partners. These structural insights contribute to a deeper understanding of p53's functional domains and the conformational changes that underlie its regulatory roles in the cell.

Phosphorylation and post-translational modification studies: The peptide serves as a substrate in kinase assays and other enzymatic studies to explore site-specific modifications within the p53 protein. By enabling controlled in vitro phosphorylation or other chemical modifications, the 139-147 fragment allows researchers to investigate the functional consequences of such modifications on p53's interactions and activity. These studies are vital for delineating the signaling pathways that regulate p53 in response to cellular stress and DNA damage, furthering the mechanistic understanding of its role in maintaining genomic integrity.

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