Peripheral Myelin Protein P2 (53-78), bovine is a segment enriched in hydrophobic and aromatic residues supporting β-structure formation. Researchers use it to probe membrane-associated folding, lipid interactions, and conformational transitions. The sequence suits studies of peripheral nerve protein analogs.
CAT No: R2416
CAS No:81628-50-4
Synonyms/Alias:Peripheral Myelin Protein P2 (53-78), bovine;81628-50-4;AKOS040758366;DA-56700;
Peripheral Myelin Protein P2 (53-78), bovine, is a synthetic peptide fragment derived from the larger P2 protein found in the myelin sheath of bovine peripheral nerves. As a segment of the P2 protein, this peptide encompasses amino acids 53 to 78, representing a region implicated in protein-lipid interactions and immunological studies. Its unique sequence and structural attributes make it a valuable research tool for investigating the molecular mechanisms underlying myelin assembly, maintenance, and function. The peptide's relevance extends to its role in myelin biology, where it serves as a model system for studying protein-peptide and protein-lipid interactions, as well as for exploring antigenic determinants involved in immune responses to myelin components. With its defined sequence and origin, Peripheral Myelin Protein P2 (53-78), bovine, is widely utilized in a variety of experimental settings, supporting fundamental research in neurobiology, immunology, and protein chemistry.
Neurobiology research: In neurobiology, the P2 (53-78) peptide is a vital tool for dissecting the molecular architecture of myelin and understanding the interactions between myelin proteins and lipids. By incorporating this peptide into in vitro systems, researchers can model the behavior of the P2 protein's functional domains and assess their role in stabilizing the myelin sheath. Its use enables the investigation of conformational changes, binding affinities, and structural dynamics that are critical for the integrity and function of peripheral nerve myelin. The ability to study these mechanisms in a controlled environment provides insights into the molecular basis of myelin-related disorders and guides the development of new hypotheses regarding myelin stability and pathology.
Immunological studies: The bovine P2 (53-78) fragment is frequently employed in immunological assays to probe antigenic epitopes recognized by immune cells. By using this peptide in T-cell proliferation assays, antibody binding studies, or epitope mapping experiments, scientists can identify regions of the P2 protein that elicit immune responses. This application is particularly valuable for elucidating the mechanisms of autoimmunity directed against myelin proteins, as well as for characterizing the specificity of antibodies generated in response to nerve injury or disease. The peptide's defined sequence facilitates precise mapping of immunodominant regions and supports the development of immunological models relevant to peripheral nerve biology.
Protein-lipid interaction analysis: The P2 (53-78) peptide serves as a model system for examining the interactions between myelin proteins and membrane lipids. Its amphipathic nature and sequence composition allow researchers to study how specific protein segments associate with lipid bilayers, micelles, or vesicles. By incorporating the peptide into biophysical assays such as surface plasmon resonance, circular dichroism, or fluorescence spectroscopy, scientists can quantify binding affinities, monitor conformational changes, and assess the factors influencing protein-membrane association. These studies advance the understanding of myelin membrane stability and the role of protein-lipid interactions in maintaining myelin structure.
Epitope mapping and antibody production: Researchers utilize the P2 (53-78) peptide for generating and characterizing antibodies against specific regions of the P2 protein. By immunizing animals or screening antibody libraries with the peptide, scientists can obtain monoclonal or polyclonal antibodies that recognize defined epitopes within the P2 domain. These antibodies are valuable reagents for studying protein localization, quantifying expression levels, and dissecting protein-protein interactions in peripheral nerves. Furthermore, the peptide facilitates the fine mapping of antigenic determinants, supporting the development of highly specific immunological tools for research applications.
Peptide-based assay development: The defined sequence and antigenic properties of the P2 (53-78) fragment make it a suitable component for developing peptide-based assays. Researchers can incorporate this peptide into ELISA, western blot, or other immunodetection platforms to measure antibody responses, monitor immune activity, or screen for protein-ligand interactions. The use of such assays enables high-throughput analysis and quantitative assessment of biological samples, supporting diverse research objectives in neurobiology and immunology. By leveraging the unique features of the P2 (53-78) peptide, scientists can design sensitive and specific assays tailored to their experimental needs, thereby advancing the study of myelin proteins and their roles in health and disease.
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