CEACAM5 is a peptide derived from a cell adhesion molecule containing residues important for β-sheet organization and receptor recognition. Researchers use it to study protein-protein interactions, folding dynamics, and surface-binding events. Its balanced hydrophobic and polar composition facilitates structural characterization.
CAT No: ta-246
CEACAM5, also known as Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, is a glycoprotein belonging to the immunoglobulin superfamily and is primarily involved in cell adhesion processes. It is widely recognized for its expression on the surface of epithelial cells, particularly in the gastrointestinal tract, and plays a significant role in intercellular communication, cellular signaling, and tissue architecture. Due to its highly regulated expression profile and functional relevance in both normal physiology and disease-associated cellular events, CEACAM5 has become a focal point in biochemical, molecular, and cellular research. Its unique structural and biochemical properties make it a valuable tool for advancing understanding in cell biology, cancer research, and immunological studies.
Biomarker research: CEACAM5 serves as a robust biomarker in various investigative contexts, especially for studies of epithelial cell differentiation, tissue-specific expression, and cellular transformation. Its differential expression in normal versus pathological tissues enables researchers to track cellular changes, investigate the molecular basis of disease progression, and assess the impact of experimental treatments in vitro. The molecule's surface localization and accessibility further facilitate the development of sensitive detection assays and imaging modalities for research use.
Cell adhesion and signaling studies: As a member of the cell adhesion molecule family, CEACAM5 is crucial for dissecting the molecular mechanisms underlying cell-cell interactions and tissue organization. Researchers employ it to elucidate the pathways involved in cellular aggregation, migration, and communication. Its role in modulating intracellular signaling cascades provides insights into the regulation of epithelial integrity, polarity, and response to external stimuli, making it indispensable in studies focused on tissue morphogenesis and homeostasis.
Antibody development and assay validation: The well-characterized epitopes and extracellular domains of CEACAM5 make it an optimal target for generating monoclonal and polyclonal antibodies. These antibodies are extensively used in the development and validation of immunoassays, including ELISA, western blotting, and immunohistochemistry, to detect and quantify the protein in various biological samples. Such assays are fundamental for basic research, experimental diagnostics, and the standardization of laboratory protocols involving epithelial markers.
Protein-protein interaction research: CEACAM5's involvement in homophilic and heterophilic binding events positions it as a key molecule for studying protein-protein interactions within the immunoglobulin superfamily and beyond. Utilizing recombinant forms or purified protein, scientists can investigate binding affinities, interaction partners, and structural determinants that govern cellular adhesion and signaling networks. These studies contribute to a broader understanding of molecular recognition and cellular communication mechanisms in complex biological systems.
Functional genomics and gene expression studies: The gene encoding CEACAM5 is frequently analyzed in functional genomics projects to explore regulatory elements, transcriptional control, and post-transcriptional modifications. Its expression profile serves as a model for investigating gene regulation in epithelial tissues and for developing reporter assays to monitor promoter activity. Such research supports the identification of factors influencing gene expression, alternative splicing events, and the interplay between genetic and epigenetic regulation in cell differentiation and disease modeling.
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