Myelin Basic Protein MBP, the second most abundant protein in central nervous system myelin, is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. Myelin Basic Protein MBP performs an important function in the peripheral nervous system (PNS).
CAT No: R1523
CAS No:126768-94-3
Synonyms/Alias:126768-94-3;Myelin Basic Protein (MBP);Myelin Basic Protein (4-14);Myelin Basic Protein MBP;Myelin Basic Protein (4-14) H-Gln-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-Tyr-Leu-OH;myelin basic protein;DTXSID90405409;H-GLN-LYS-ARG-PRO-SER-GLN-ARG-SER-LYS-TYR-LEU-OH;DA-55790;Glutaminyllysyl-N~5~-(diaminomethylidene)ornithylprolylserylglutaminyl-N~5~-(diaminomethylidene)ornithylseryllysyltyrosylleucine;NCCCCC(NC(C(CCC(N)=O)N)=O)C(NC(C(N1CCCC1C(NC(CO)C(NC(CCC(N)=O)C(NC(CCCNC(N)=N)C(NC(CO)C(NC(CCCCN)C(NC(CC2=CC=C(O)C=C2)C(NC(C(O)=O)CC(C)C)=O)=O)=O)=O)=O)=O)=O)=O)CCCNC(N)=N)=O;
Myelin Basic Protein MBP is a highly conserved, intrinsically disordered protein that plays a central role in the structure and function of the myelin sheath within the central nervous system. As a major constituent of myelin, MBP is critical for the compaction, stabilization, and maintenance of myelin membranes, thereby ensuring efficient nerve impulse conduction. Its unique biochemical properties, including strong charge interactions and membrane-binding capabilities, have made it a focal point for research in neurobiology, demyelinating diseases, and membrane-protein interactions. The availability of purified MBP supports a diverse array of experimental approaches aimed at elucidating myelin biology and the molecular mechanisms underlying neurological disorders.
Neuroscience research: MBP is extensively utilized as a molecular tool in studies investigating the biology of myelination and demyelination. Researchers employ it to model the assembly and maintenance of myelin in vitro, enabling detailed examination of the molecular interactions responsible for myelin sheath formation. Its role as a marker protein also facilitates the identification and quantification of myelinated fibers in tissue samples, supporting investigations into neurodevelopmental processes and the impact of genetic or environmental perturbations on myelin integrity.
Autoimmunity and multiple sclerosis studies: The protein serves as a key antigen in experimental models of autoimmune demyelination, most notably in the induction of experimental autoimmune encephalomyelitis (EAE). By introducing MBP into animal models, scientists can mimic aspects of multiple sclerosis pathogenesis, providing a platform for dissecting immune responses against myelin components. These studies are instrumental in advancing the understanding of T-cell mediated mechanisms, antigen processing, and the development of potential immunomodulatory strategies.
Protein-membrane interaction assays: Due to its strong affinity for lipid membranes, MBP is frequently employed in biophysical and biochemical assays that explore the dynamics of protein-lipid interactions. In vitro reconstitution experiments utilize the protein to investigate membrane compaction, charge-mediated binding, and the effects of post-translational modifications on membrane association. These assays yield valuable insights into the basic principles of membrane organization and the structural determinants of protein-lipid interplay.
Analytical reference standard: MBP serves as a reliable standard in a range of analytical techniques, including immunoblotting, enzyme-linked immunosorbent assays (ELISA), and mass spectrometry. Its well-characterized sequence and immunogenic properties make it an ideal positive control for assay validation, antibody specificity testing, and quantitative protein analysis. Employing MBP as a reference material enhances the reproducibility and interpretability of experimental results in both academic and industrial laboratory settings.
Recombinant protein expression studies: The protein is widely used as a fusion tag in recombinant protein expression systems, particularly in bacterial hosts. MBP-fusion constructs facilitate the solubility and purification of heterologous proteins, overcoming challenges associated with aggregation and misfolding. This application is valuable for structural biology, functional characterization, and the production of challenging target proteins, streamlining downstream purification workflows and improving overall yield and quality.
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