p53 (17-26) is amino acids 17 to 26 fragment of p53. p53 (17-26) is mdm-2-binding domain.
p53 17-26 is a synthetic peptide fragment corresponding to amino acid residues 17 through 26 of the human p53 tumor suppressor protein. As a well-characterized segment within the N-terminal transactivation domain, this decapeptide plays a pivotal role in mediating protein-protein interactions central to p53 function. Researchers value this fragment for its ability to model crucial aspects of p53 signaling, regulatory mechanisms, and structural interactions, making it an indispensable tool in molecular biology, cancer research, and peptide biochemistry. Its defined sequence enables precise experimental manipulation, facilitating studies into the mechanistic underpinnings of cell cycle control and apoptosis.
Protein-protein interaction studies: The p53 17-26 peptide is widely used to investigate the molecular interactions between p53 and its regulatory partners, such as MDM2 and MDMX. The N-terminal region represented by this peptide contains a conserved motif essential for binding to these negative regulators, which modulate p53 stability and activity. By employing this fragment in binding assays or competition experiments, researchers can dissect the affinity and specificity of these interactions, providing insights into the regulation of p53-dependent cellular responses.
Structural biology and biophysical analysis: As a model system, the peptide serves as a valuable tool for structural studies using techniques like nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and surface plasmon resonance. Its well-defined sequence allows scientists to elucidate the conformational properties and binding interfaces involved in p53's interactions with other macromolecules. Such studies are instrumental in mapping key recognition motifs and understanding the dynamic behavior of intrinsically disordered regions within the full-length protein.
Peptide inhibitor development: The 17-26 sequence of p53 is frequently utilized as a template for designing and optimizing peptide-based inhibitors targeting the p53-MDM2/MDMX interaction. By systematically modifying this peptide, researchers can assess structure-activity relationships and identify analogs with enhanced binding affinity or altered specificity. These efforts support the development of novel molecular probes and chemical biology tools to modulate p53 signaling in a controlled experimental context.
Cellular signaling pathway elucidation: The synthetic peptide provides a means to probe p53-dependent signaling cascades in cell-free systems or cellular extracts. By introducing the fragment into biochemical assays, scientists can monitor its effects on downstream effectors, transcriptional activity, or ubiquitination processes. This approach helps clarify the functional consequences of disrupting or mimicking the native p53 interactions, advancing the understanding of its regulatory network in normal and stressed cells.
Analytical tool for antibody validation: The defined sequence of p53 17-26 makes it a reliable standard for validating the specificity and sensitivity of antibodies directed against the N-terminal domain of p53. Researchers can employ the peptide in immunoassays, such as ELISA or Western blotting, to confirm antibody recognition and minimize off-target detection. This application is crucial for ensuring the accuracy and reproducibility of experimental data in studies involving p53 detection and quantification.
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