Coiled-coil and C2 domain-containing protein 2A isoform a (1275-1287)

Coiled-coil and C2 domain-containing protein 2A isoform a (1275-1287) is a synthetic peptide fragment derived from the C-terminal region of the CC2D2A protein. This peptide sequence encompasses amino acids 1275 to 1287, a region implicated in the structural and functional organization of the parent protein, which is known for its roles in membrane trafficking, ciliogenesis, and protein-protein interactions. As a well-characterized peptide segment, it provides a focused tool for dissecting the molecular mechanisms underlying the activity and regulation of CC2D2A, particularly in studies targeting the functional domains responsible for cellular localization and signaling events.

Epitope mapping: The peptide corresponding to residues 1275-1287 of CC2D2A serves as a valuable reagent for epitope mapping and antibody characterization. Researchers can utilize this defined sequence to generate or validate antibodies specific to the C-terminal region of CC2D2A, supporting the development of highly specific detection tools for immunoblotting, immunoprecipitation, or immunofluorescence. This application is critical for distinguishing between isoforms and assessing protein localization or abundance in diverse biological samples.

Protein-protein interaction studies: The 1275-1287 peptide fragment enables targeted investigation of protein-protein interaction interfaces within the CC2D2A network. By serving as a competitive inhibitor or probe in binding assays, it helps elucidate the molecular determinants of CC2D2A-mediated complexes, especially those involving coiled-coil and C2 domain interactions. Such studies provide mechanistic insights into the assembly and regulation of multiprotein complexes essential for cellular signaling and structural integrity.

Functional domain analysis: Incorporating the synthetic peptide into functional assays allows researchers to dissect the specific contributions of the C-terminal segment to the overall activity of CC2D2A. Site-directed mutagenesis and peptide competition experiments can reveal how this region influences membrane association, subcellular targeting, or downstream signaling pathways. These approaches are instrumental in mapping structure-activity relationships within the protein and identifying critical residues involved in its biological function.

Post-translational modification research: The defined sequence of the 1275-1287 region offers a suitable substrate for investigating potential post-translational modifications, such as phosphorylation, ubiquitination, or acetylation. In vitro modification assays and mass spectrometry analysis using this peptide enable precise identification of modification sites and their regulatory impact on CC2D2A function. This application supports broader efforts to understand dynamic regulatory mechanisms affecting protein activity and cellular processes.

Peptide-based assay development: The synthetic peptide can be integrated into customized assay platforms designed to monitor the presence, modification, or interaction of CC2D2A or its partners. By providing a standardized and reproducible reagent, it facilitates the optimization of quantitative assays, such as ELISA or surface plasmon resonance, which are essential for high-throughput screening and detailed kinetic studies. These applications contribute to advancing research in cell biology, molecular signaling, and the development of analytical tools for protein characterization.

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