Carcinoembryonic antigen-related cell adhesion molecule 5 (355-367)

Carcinoembryonic antigen-related cell adhesion molecule 5 (355-367) is a synthetic peptide fragment derived from the CEA-related cell adhesion molecule 5, a glycoprotein prominently involved in intercellular adhesion and tumor biology. This peptide segment represents a specific epitope within the larger CEACAM5 protein, which is highly expressed in various epithelial tissues and overexpressed in several carcinomas. Its defined amino acid sequence and origin make it a valuable molecular tool for elucidating protein-protein interactions, mapping antibody epitopes, and advancing research into the mechanisms of cell adhesion, signaling, and tumor progression.

Epitope mapping: The 355-367 peptide fragment serves as a precise probe for identifying and characterizing antibody binding sites within the CEACAM5 molecule. Researchers utilize this defined sequence to assess the specificity and affinity of monoclonal or polyclonal antibodies, supporting the development of highly selective detection reagents. Such mapping studies are essential for understanding immune recognition, optimizing antibody-based assays, and guiding the design of targeted diagnostic tools.

Immunoassay development: As an antigenic peptide, the 355-367 region of CEACAM5 is frequently incorporated into immunoassay systems, including ELISA and western blot protocols. Its use as a coating antigen or competitive binding substrate enables the quantification and monitoring of anti-CEACAM5 antibody responses in various biological samples. This application is particularly relevant in research settings focused on tumor marker detection, immune profiling, and the evaluation of humoral responses in experimental models.

Peptide-based inhibitor studies: The synthetic 355-367 peptide allows investigation into the molecular determinants of cell adhesion and signaling mediated by CEACAM5. By serving as a competitive inhibitor or binding competitor in in vitro assays, it facilitates the dissection of protein-protein interactions critical to cellular communication and metastatic processes. Researchers leverage this approach to delineate the functional domains of CEACAM5 and to explore strategies for modulating its activity in the context of cancer research.

T-cell epitope analysis: The defined sequence of the 355-367 fragment provides a platform for studying T-cell recognition and antigen presentation mechanisms. Investigators employ this peptide to stimulate peripheral blood mononuclear cells or T-cell clones in vitro, enabling the identification of immunodominant epitopes and the characterization of cellular immune responses. Insights gained from such studies inform the understanding of tumor immunology and support the rational design of peptide-based vaccines or immunotherapeutic candidates.

Biochemical assay calibration: The 355-367 peptide is also utilized as a standard or calibrator in a range of biochemical assays investigating CEACAM5 function and expression. Its high sequence fidelity and reproducibility ensure consistent results in quantitative analyses, such as mass spectrometry-based proteomics or peptide quantification studies. By providing a reliable reference, the peptide supports assay validation and enhances the accuracy of experimental workflows focused on cell adhesion molecules.

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