Epithelial cell adhesion molecule
Epithelial cell adhesion molecule (173-181) is a synthetic peptide fragment derived from the extracellular domain of the human EpCAM protein, a well-characterized transmembrane glycoprotein involved in cell-cell adhesion, proliferation, and differentiation within epithelial tissues. This specific peptide sequence, corresponding to amino acids 173 through 181, is of particular interest in biochemical and cell biology research due to its relevance in mediating protein-protein interactions and its utility as an epitope for antibody recognition studies. As a defined peptide segment, it provides a valuable tool for dissecting the structural and functional aspects of EpCAM, facilitating detailed investigations into epithelial cell behavior, signaling mechanisms, and molecular recognition processes.
Epitope mapping: The (173-181) peptide fragment is frequently employed in epitope mapping experiments to identify and characterize the binding sites of monoclonal and polyclonal antibodies raised against EpCAM. By providing a defined linear sequence, this peptide enables researchers to delineate the specific regions of the parent protein that are recognized by immune reagents, supporting the development and validation of antibody-based detection systems. Such studies are essential for refining immunoassays, improving antibody specificity, and advancing diagnostic research tools targeting epithelial markers.
Protein interaction studies: As a representative segment of the EpCAM extracellular domain, this peptide facilitates the investigation of protein-protein interactions implicated in epithelial cell adhesion and signaling. Researchers utilize the fragment in binding assays, surface plasmon resonance, or pull-down experiments to probe the affinity and specificity of interacting partners, including other cell adhesion molecules or extracellular ligands. These applications provide mechanistic insights into the molecular determinants governing cell-cell communication and tissue organization in epithelial biology.
Peptide-based assay development: The defined sequence of the (173-181) peptide supports the design and optimization of peptide-based assays, such as enzyme-linked immunosorbent assays (ELISA) or competitive binding formats. Its use as a standard or competitor enables quantitative and qualitative measurement of EpCAM-targeted antibodies or ligands in biological samples. Such assays are instrumental in biomarker discovery, antibody screening, and the assessment of reagent performance in research and development workflows.
Structural and conformational analysis: The synthetic peptide serves as a model system for exploring the structural and conformational properties of EpCAM's extracellular regions. Spectroscopic techniques, such as circular dichroism or nuclear magnetic resonance, can be employed to analyze the secondary structure propensity of the peptide in solution, providing foundational data for understanding how specific sequence motifs contribute to the overall folding and function of the full-length protein. These structural studies are crucial for guiding mutagenesis experiments and rational design of peptide mimetics.
Peptide functionalization and conjugation: The (173-181) fragment is amenable to chemical modification and conjugation strategies, making it suitable for the generation of peptide probes, affinity tags, or bioconjugates. Researchers can couple the peptide to carrier proteins, labels, or solid supports to create reagents for affinity purification, imaging, or biosensor applications. Such functionalized peptides expand the toolkit available for targeted isolation, detection, and analysis of EpCAM-related molecules in complex biological samples, supporting a wide range of experimental approaches in molecular and cellular research.
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