Carcinoembryonic antigen-related cell adhesion molecule 5 (268-277)

Carcinoembryonic antigen-related cell adhesion molecule 5 (268-277) is a synthetic peptide fragment derived from the larger CEACAM5 protein, a member of the immunoglobulin superfamily known for its roles in cell adhesion and intercellular signaling. This specific sequence corresponds to amino acids 268 through 277 of CEACAM5, a region that may be involved in protein-protein interactions, epitope mapping, or functional modulation within the CEACAM family. Due to its defined structure and biological relevance, the peptide serves as a valuable tool in molecular biology, immunology, and cancer research, enabling precise interrogation of CEACAM5's functional domains and their implications in cellular processes.

Peptide epitope mapping: Researchers utilize the 268-277 fragment of CEACAM5 to map antibody binding sites and characterize epitope specificity. By employing this peptide in immunoassays or binding studies, investigators can determine which regions of the full-length CEACAM5 molecule are recognized by monoclonal or polyclonal antibodies. Such insights are critical for developing highly specific detection reagents, optimizing immunohistochemical protocols, and advancing antibody-based research tools targeting CEACAM5.

Protein-protein interaction studies: The defined 268-277 peptide sequence provides a model substrate for probing the molecular interactions between CEACAM5 and its physiological partners. In vitro assays employing this fragment allow for the dissection of binding affinities, kinetic parameters, and structural determinants underlying CEACAM-mediated adhesion or signaling. These studies contribute to a deeper understanding of how CEACAM5 interfaces with other cell surface molecules, which is relevant in contexts such as tissue organization, immune modulation, and tumor progression.

T-cell response analysis: In immunological research, the CEACAM5 (268-277) peptide is used to assess cellular immune responses, particularly in the context of antigen presentation and T-cell activation. By loading this peptide onto antigen-presenting cells or incorporating it into ex vivo stimulation assays, scientists can evaluate the specificity and magnitude of T-cell recognition directed against CEACAM5-derived epitopes. This approach is instrumental in elucidating mechanisms of immune surveillance and tolerance in cancer and other pathological conditions where CEACAM5 is expressed.

Peptide-based assay development: The synthetic nature and defined sequence of the 268-277 fragment make it suitable for incorporation into various biochemical and analytical assays. It can serve as a standard or calibrator in quantitative peptide detection methods, facilitate the development of competitive binding assays, or act as a substrate for enzymatic modification studies. These applications support the advancement of robust, reproducible experimental platforms for investigating CEACAM5 biology.

Peptide synthesis and modification research: The 268-277 sequence offers a practical model for exploring strategies in solid-phase peptide synthesis, post-synthetic modification, and structure-activity relationship analysis. Researchers may use this peptide to optimize coupling conditions, introduce site-specific modifications such as labeling or conjugation, and evaluate the impact of sequence alterations on structural stability or biological function. Such work underpins the broader field of peptide engineering and supports the creation of tailored reagents for advanced biochemical investigations.

1. Olfactory receptor based piezoelectric biosensors for detection of alcohols related to food safety applications

2. Oleic acid and glucose regulate glucagon-like peptide 1 receptor expression in a rat pancreatic ductal cell line

3. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum

4. Relatedness of antibodies to peptides containing homocitrulline or citrulline in patients with rheumatoid arthritis

5. Characterization of Novel P-Selectin Targeted Complement Inhibitors in Murine Models of Hindlimb Injury and Transplantation