Rad17 Derived Peptide represents a segment of the Rad17 protein used to investigate checkpoint signaling and protein-protein interfaces. Polar, charged, and hydrophobic residues contribute to structured recognition. Researchers employ it in binding assays and phosphorylation-related studies. Applications include DNA-damage pathway research, motif-function analysis, and structural modeling.
CAT No: R2824
Synonyms/Alias:Rad17 derived peptide; SP-050; SP050; ASELPASQPQPFSAKKK
Rad17 derived peptide is a synthetic peptide fragment modeled after sequences from the Rad17 protein, a key player in the DNA damage response pathway. As a component of the checkpoint clamp loader complex, Rad17 is essential for the activation of cell cycle checkpoints in response to genotoxic stress, ensuring genomic stability and proper DNA repair. The derived peptide is designed to mimic specific functional motifs of the native Rad17 protein, making it a versatile tool for dissecting protein-protein interactions, post-translational modifications, and checkpoint signaling mechanisms in various biochemical and cellular contexts. Its well-defined sequence and structural properties allow for precise manipulation in experimental systems, facilitating detailed studies of DNA damage sensing and repair pathways.
Protein interaction studies: Rad17-derived peptides are frequently employed to investigate the molecular interactions between Rad17 and its binding partners, such as components of the 9-1-1 complex or replication factor C (RFC) subunits. By serving as a competitive inhibitor or affinity probe in pulldown assays, surface plasmon resonance, or co-immunoprecipitation experiments, the peptide enables researchers to map interaction domains, determine binding affinities, and elucidate the structural basis of checkpoint complex assembly. These insights are critical for understanding how cells coordinate DNA repair processes and maintain genomic integrity under stress conditions.
Phosphorylation and post-translational modification analysis: The peptide is often used as a substrate or reference standard in kinase assays and mass spectrometry-based studies focused on Rad17 phosphorylation sites. By incorporating specific serine or threonine residues that are targets for checkpoint kinases such as ATR or ATM, the peptide allows for the quantitative assessment of phosphorylation dynamics, kinase specificity, and the regulatory impact of these modifications on checkpoint activation. Such applications are invaluable for unraveling the signaling cascades that control cell cycle progression in response to DNA damage.
Antibody validation and epitope mapping: Researchers utilize Rad17-derived peptides to generate and validate antibodies that recognize defined regions or post-translationally modified forms of the Rad17 protein. In immunoblotting, ELISA, or immunoprecipitation assays, the peptide serves as a positive control or blocking agent to confirm antibody specificity and sensitivity. Additionally, it facilitates the precise mapping of antibody epitopes, supporting the development of high-quality immunoreagents for use in cell biology and DNA repair research.
Peptide-based inhibitor development: As a mimic of functional domains within Rad17, the peptide can be utilized in screening assays to identify small molecules or other peptides that disrupt critical protein-protein interactions within the checkpoint machinery. These inhibitor discovery efforts contribute to the broader understanding of checkpoint regulation and may inform the design of novel research tools for modulating DNA damage response pathways in experimental systems.
Structural and biophysical characterization: The defined sequence and accessible size of the Rad17-derived peptide make it suitable for NMR spectroscopy, circular dichroism, or crystallography studies aimed at elucidating secondary structure, conformational dynamics, or molecular recognition features. Such structural investigations provide atomic-level insights into the determinants of checkpoint protein function, informing mutagenesis strategies and the rational design of functional analogs for further mechanistic studies.
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