Cellular tumor antigen p53 (99-107)

Cellular tumor antigen p53

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-381

Synonyms/Alias:Cellular tumor antigen p53 (99-107)

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Sequence
SQKTYQGSY
Areas of Interest
Antigen-presenting Cells; Cancer Research

Cellular tumor antigen p53 (99-107) is a synthetic peptide fragment corresponding to amino acid residues 99 to 107 of the human p53 protein, a pivotal tumor suppressor involved in cell cycle regulation, DNA repair, and apoptosis. This peptide segment is derived from a highly conserved region of p53, making it a valuable tool for research into protein-protein interactions, post-translational modifications, and the molecular mechanisms underlying tumorigenesis. Its defined sequence and structural features enable precise investigations into the functional domains of p53, supporting studies that aim to elucidate the complex regulatory networks governing cellular responses to genomic stress and oncogenic transformation.

Epitope mapping: Researchers utilize the p53 (99-107) peptide for detailed epitope mapping studies, particularly in the context of antibody development and immune recognition. By providing a well-defined linear epitope from the central region of the p53 protein, the peptide serves as a reference substrate for characterizing monoclonal and polyclonal antibody specificity. This application is instrumental in the validation and optimization of immunoassays, such as ELISA and Western blotting, where accurate detection of p53 or its fragments is critical for experimental reproducibility and data interpretation.

Protein interaction studies: The 99-107 fragment is frequently employed to probe the binding interactions between p53 and its cellular partners. Its sequence encompasses residues implicated in intramolecular contacts and interactions with regulatory proteins, such as MDM2 and other modulators of p53 stability and activity. By incorporating this peptide into binding assays, surface plasmon resonance experiments, or pull-down protocols, investigators can dissect the molecular determinants of p53 regulation, identify novel interacting factors, and assess the impact of post-translational modifications on binding affinity.

Peptide-based assay development: The defined nature of the p53 (99-107) peptide makes it an excellent standard or control for the development and calibration of quantitative peptide-based assays. In mass spectrometry workflows, for example, it is used as a reference peptide to optimize instrument parameters, validate peptide identification protocols, and quantify endogenous p53 fragments within complex biological samples. This contributes to enhanced assay sensitivity and specificity in proteomic analyses focused on tumor suppressor pathways.

T-cell immunogenicity research: The sequence corresponding to residues 99-107 of p53 contains motifs recognized by human leukocyte antigen (HLA) molecules, rendering it relevant for studies of antigen processing and presentation. Immunologists employ this peptide to investigate T-cell responses against p53-derived epitopes, particularly in the context of tumor immunology and neoantigen discovery. Such research informs the understanding of immune surveillance mechanisms and the development of novel immunotherapeutic strategies targeting aberrant p53 expression in cancer cells.

Phosphorylation and post-translational modification analysis: The 99-107 region of p53 is subject to regulatory phosphorylation events that modulate protein function and cellular localization. Synthetic peptides corresponding to this segment are utilized as substrates in kinase assays, enabling researchers to characterize site-specific phosphorylation patterns and their functional consequences. By serving as precise biochemical tools, these peptides facilitate the dissection of signaling pathways that converge on the p53 axis, advancing knowledge of cellular stress responses and the molecular etiology of cancer.

Source#
Homo sapiens (human)
Epitope
99-107
Restricting HLA
HLA-B46
References
Azuma; Cancer Res 2003

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