Carcinoembryonic antigen-related cell adhesion molecule 5 (666-678)

Carcinoembryonic antigen-related cell adhesion molecule 5 (666-678) is a synthetic peptide fragment derived from the CEACAM5 protein, a member of the immunoglobulin superfamily involved in cellular adhesion processes. As a defined sequence peptide corresponding to residues 666 through 678 of the CEACAM5 molecule, it serves as a valuable molecular tool for researchers investigating the structural and functional aspects of cell adhesion molecules. The sequence's relevance is underscored by its role in mediating intercellular interactions, modulating signal transduction pathways, and serving as a model epitope for immunological studies. Its biochemical properties make it particularly suitable for applications in peptide-based assays, antibody generation, and mechanistic studies of cell adhesion and recognition.

Epitope mapping: The defined sequence of this CEACAM5 fragment is ideal for mapping antibody binding sites and characterizing immune recognition. Researchers utilize the peptide in immunological assays to determine the specificity and affinity of monoclonal or polyclonal antibodies targeting the CEACAM5 protein. This approach is fundamental in the development and validation of immunodetection reagents, as well as in elucidating the molecular determinants of antigen-antibody interactions.

Antibody production: The peptide serves as a potent immunogen for the generation of sequence-specific antibodies. By conjugating the fragment to carrier proteins, immunologists can raise highly selective antibodies that recognize the 666-678 epitope within the larger CEACAM5 molecule. These antibodies are widely employed in research for the detection, quantification, and localization of CEACAM5 in various biological samples, supporting both basic and applied studies in cell biology and oncology.

Peptide-based assay development: The synthetic nature and defined sequence of the CEACAM5 (666-678) peptide make it a valuable standard or control in assay systems. It is frequently incorporated into enzyme-linked immunosorbent assays (ELISA), western blots, or immunoprecipitation protocols to calibrate assay sensitivity, validate specificity, and optimize detection parameters. Such uses are critical for ensuring reproducibility and accuracy in quantitative and qualitative protein analyses.

Cell adhesion studies: As a functional motif derived from a cell adhesion molecule, the peptide provides a tractable model for dissecting the molecular mechanisms underlying cell-cell interactions. Researchers employ the fragment in in vitro assays to probe the roles of specific CEACAM5 domains in mediating adhesion, migration, or signal transduction. These studies contribute to a deeper understanding of cellular communication processes and the regulation of tissue architecture.

Protein-protein interaction research: The sequence corresponding to residues 666-678 offers a focused probe for investigating direct and indirect interactions between CEACAM5 and its binding partners. By incorporating the peptide into binding assays or structural studies, scientists can identify interacting domains, characterize binding affinities, and elucidate the structural basis of molecular recognition events. Such insights are instrumental in advancing the knowledge of adhesion molecule networks and their biological significance.

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