Cellular tumor antigen p53
CAT No: ta-088
Synonyms/Alias:P53_HUMAN Cellular tumor antigen p53 (Tumor suppressor p53) (Phosphoprotein p53) (Antigen NY-CO-13) (187-197)
NY-CO-13(187-197) is a synthetic peptide fragment derived from the NY-CO-13 protein, also known as cancer/testis antigen 13. As a defined sequence peptide, it represents a specific epitope region spanning amino acids 187 to 197 within the parent protein. This segment is of particular interest in immunological and cancer research due to its restricted expression profile and potential involvement in cellular processes relevant to tumor biology. The peptide's well-characterized structure and sequence specificity make it a valuable tool for dissecting molecular interactions, mapping antigenic determinants, and supporting the development of targeted assays in experimental settings.
Epitope mapping: Utilization of the NY-CO-13(187-197) peptide enables precise delineation of linear B-cell or T-cell epitopes within the NY-CO-13 antigen. By incorporating this defined fragment into immunoassays or screening platforms, researchers can systematically evaluate antibody or T-cell receptor recognition patterns, facilitating the identification of immunodominant regions. This approach aids the development of more refined reagents for immunodetection and supports the fundamental understanding of antigenicity in the context of tumor-associated antigens.
Antibody validation: The peptide serves as a reliable positive control or antigenic substrate in antibody generation and validation studies. By employing NY-CO-13(187-197) in ELISA, Western blot, or immunoprecipitation assays, investigators can quantitatively assess the specificity and affinity of monoclonal or polyclonal antibodies raised against the NY-CO-13 protein. Such validation is essential for ensuring reagent accuracy in downstream applications, including biomarker discovery and basic research involving cancer/testis antigens.
Peptide-based assay development: As a chemically defined analyte, NY-CO-13(187-197) is well-suited for the calibration and optimization of peptide-based detection platforms. Its use in assay development allows for the fine-tuning of detection limits, specificity, and reproducibility in systems designed to monitor immune responses or antigen presence. This capability is particularly valuable in the creation of high-throughput screening assays, multiplex immunoassays, or peptide microarrays targeting cancer-associated antigens.
Functional studies of antigen presentation: The peptide fragment provides a controlled substrate for evaluating antigen processing and presentation by major histocompatibility complex (MHC) molecules. By loading NY-CO-13(187-197) onto antigen-presenting cells or synthetic MHC complexes, researchers can investigate the efficiency and specificity of peptide-MHC binding, T-cell activation, and downstream signaling events. These studies contribute to a deeper understanding of immune recognition mechanisms and inform the rational design of immunological research tools.
Structural and biophysical analysis: NY-CO-13(187-197) supports detailed investigations into peptide conformation, stability, and molecular interactions using techniques such as NMR spectroscopy, circular dichroism, or surface plasmon resonance. By analyzing the structural properties of this defined sequence, scientists can elucidate the factors governing peptide folding, binding kinetics, and interaction with antibodies or cellular receptors. Such insights are instrumental in guiding the rational design of peptide analogs or modified immunoreagents for advanced research applications.
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