NY-CO-13 (139-147)

NY-CO-13 (139-147) is a synthetic peptide fragment derived from the NY-CO-13 protein, also known as a cancer/testis antigen with restricted expression in normal tissues but elevated presence in various malignancies. This peptide, corresponding to amino acids 139 through 147 of the parent protein, is frequently utilized in immunological and oncological research due to its well-defined sequence and antigenic properties. Its biochemical relevance lies in its ability to mimic a naturally occurring epitope, making it a valuable reagent for studying immune recognition, antigen processing, and peptide-MHC interactions. The fragment's sequence specificity, stability, and compatibility with standard peptide handling protocols further enhance its utility in experimental workflows focused on tumor antigen discovery and T-cell response characterization.

Epitope Mapping: Researchers employ this peptide fragment for detailed epitope mapping, particularly within the context of tumor antigen recognition. By using the defined 139-147 sequence, investigators can systematically assess T-cell or antibody specificity toward the NY-CO-13 antigen. Such studies are critical for delineating the precise regions of the full-length protein that are immunologically relevant, thereby informing the selection of candidate epitopes for further immunological or therapeutic investigation. The peptide's synthetic nature ensures batch-to-batch consistency, which is essential for reproducible mapping studies.

T-Cell Activation Assays: The peptide serves as a robust tool in T-cell activation assays, where it is used to stimulate antigen-specific cytotoxic T lymphocytes (CTLs) derived from peripheral blood or tumor-infiltrating lymphocytes. By presenting the 139-147 epitope in the context of appropriate major histocompatibility complex (MHC) molecules, researchers can quantify T-cell responses via cytokine production, proliferation, or cytolytic activity. These assays are vital for evaluating the immunogenicity of cancer/testis antigens and for assessing the functional competence of patient-derived immune cells in preclinical studies.

Peptide-MHC Binding Studies: The defined amino acid sequence of this fragment allows for precise investigation of peptide-MHC binding affinity and stability. Using in vitro binding assays, scientists can evaluate how efficiently the 139-147 epitope associates with various class I or class II MHC alleles. Such studies provide insight into the molecular determinants of antigen presentation and inform the rational design of immunotherapeutic approaches targeting NY-CO-13 or related antigens. The results can also guide the selection of optimal peptide candidates for vaccine development or adoptive cell transfer protocols.

Antibody Generation and Characterization: The peptide is frequently used as an immunogen for the generation of monoclonal or polyclonal antibodies specific to the NY-CO-13 139-147 epitope. These antibodies are instrumental in detecting the presence and distribution of the parent antigen in tissue samples, cell lysates, or other biological matrices. Furthermore, the peptide enables affinity purification and fine specificity testing of antibody preparations, supporting downstream applications such as immunohistochemistry, western blotting, and flow cytometry.

Analytical Method Development: Analytical laboratories utilize the 139-147 peptide fragment as a reference standard or positive control in the development and validation of peptide quantification assays, including mass spectrometry-based workflows. Its defined sequence and physicochemical properties facilitate calibration, sensitivity assessment, and method optimization, ensuring accurate detection of NY-CO-13-derived peptides in complex biological samples. This capability is particularly valuable in biomarker discovery, pharmacokinetic studies, and quality control processes within research and development settings.

1. Implications of ligand-receptor binding kinetics on GLP-1R signalling

2. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I

3. Constitutive and inflammation-dependent antimicrobial peptides produced by epithelium are differentially processed and inactivated by the commensal Finegoldia magna and the pathogen Streptococcus pyogenes

4. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle

5. Oleic acid and glucose regulate glucagon-like peptide 1 receptor expression in a rat pancreatic ductal cell line