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 peripheral myelin protein P2, a key structural component of the myelin sheath in the peripheral nervous system. The 53-78 amino acid sequence represents a functionally significant region implicated in lipid binding and membrane stabilization, making it a valuable tool for neurobiological and biochemical studies. As a research-use peptide, it provides a precise model for investigating the molecular interactions and structural dynamics of myelin proteins, offering insights into nerve physiology and the mechanisms underlying myelin-associated processes.
Myelin Structure and Function Studies: Researchers employ the P2 (53-78) peptide fragment to dissect the structural and functional roles of peripheral myelin protein domains within the myelin sheath. By isolating this specific sequence, scientists can study its direct interactions with lipid membranes and other myelin components, thereby elucidating the contributions of P2 to myelin compaction, stability, and overall nerve insulation. Such investigations are crucial for advancing the understanding of peripheral nerve biology and the molecular architecture of myelinated fibers.
Protein-Lipid Interaction Analysis: The peptide serves as a model system for detailed biophysical and biochemical assays focused on protein-lipid binding mechanisms. Its amphipathic nature and sequence-specific properties allow for in vitro studies that characterize how myelin proteins associate with phospholipid bilayers and fatty acids. These analyses help clarify the molecular determinants of membrane affinity and specificity, informing broader research into membrane protein function and the biogenesis of myelin structures.
Epitope Mapping and Antibody Development: The defined sequence of the P2 (53-78) peptide enables its use as an epitope in immunological studies. Researchers utilize the fragment to map antibody binding sites, validate immunoreagents, or generate sequence-specific polyclonal or monoclonal antibodies. Such applications are instrumental in developing robust tools for detecting peripheral myelin protein P2 in tissue samples, western blots, or immunohistochemical assays, thereby supporting a wide range of neurobiological research objectives.
Peptide-Protein Interaction Screening: The synthetic peptide is frequently integrated into binding assays to identify and characterize protein partners that interact with the P2 region. By immobilizing or labeling the fragment, scientists can screen for proteins, peptides, or small molecules that recognize or modulate this domain, shedding light on regulatory pathways and potential modulators of myelin assembly or maintenance. These studies contribute to a deeper understanding of the molecular networks governing peripheral nerve function.
Peptide Synthesis and Analytical Method Development: As a well-defined peptide standard, the P2 (53-78) fragment is valuable for optimizing and validating peptide synthesis protocols, chromatographic separation techniques, and mass spectrometry-based analytical methods. Its use as a reference compound supports the calibration of instrumentation and the assessment of peptide purity, sequence fidelity, and post-synthetic modifications. Such methodological applications are essential for ensuring accuracy and reproducibility in peptide-based research workflows.
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