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Mouse Anti-MBP Recombinant Antibody (CBMAB-BR345LY)


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Summary

Host Animal
Mouse
Specificity
Cattle, Horse, Human, Mouse, Pig, Rat
Antibody Isotype
IgG
Application
IF: 1:1000 dilution, WB: 0.1-0.5 μg/ml

Basic Information

Immunogen
Purified myelin basic protein isolated from bovine brain
Specificity
Cattle, Horse, Human, Mouse, Pig, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
50% glycerol
Preservative
5mM sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
MAP3K12 Binding Inhibitory Protein 1
Introduction
The protein encoded by the classic MBP gene is a major constituent of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system. However, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs arise from the long MBP gene (otherwise called "Golli-MBP") that contains 3 additional exons located upstream of the classic MBP exons. Alternative splicing from the Golli and the MBP transcription start sites gives rise to 2 sets of MBP-related transcripts and gene products. The Golli mRNAs contain 3 exons unique to Golli-MBP, spliced in-frame to 1 or more MBP exons. They encode hybrid proteins that have N-terminal Golli aa sequence linked to MBP aa sequence. The second family of transcripts contain only MBP exons and produce the well characterized myelin basic proteins. This complex gene structure is conserved among species suggesting that the MBP transcription unit is an integral part of the Golli transcription unit and that this arrangement is important for the function and/or regulation of these genes. [provided by RefSeq, Jul 2008]
Entrez Gene ID
Human4155
Mouse17196
Rat24547
Pig414286
Cattle618684
Horse100063306
UniProt ID
HumanP02686
MouseP04370
RatP02688
PigP81558
CattleP02687
HorseP83487
Alternative Names
Myelin basic protein;MBP;Myelin A1 protein;Mbp;Shi;
Function
The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation.
Biological Process
Aging Source: Ensembl
Axon ensheathment Source: ProtInc
Central nervous system development Source: ProtInc
Chemical synaptic transmission Source: ProtInc
Immune response Source: ProtInc
Maintenance of blood-brain barrier Source: CAFA
MAPK cascade Source: CAFA
Membrane organization Source: Ensembl
Myelination Source: GO_Central
Negative regulation of axonogenesis Source: Ensembl
Negative regulation of heterotypic cell-cell adhesion Source: CAFA
Positive regulation of chemokine (C-X-C motif) ligand 2 production Source: CAFA
Positive regulation of interleukin-6 production Source: CAFA
Positive regulation of metalloendopeptidase activity Source: CAFA
Response to fatty acid Source: Ensembl
Response to mercury ion Source: Ensembl
Response to progesterone Source: Ensembl
Response to toxic substance Source: Ensembl
Response to tumor necrosis factor Source: Ensembl
Sensory perception of sound Source: Ensembl
Substantia nigra development Source: UniProtKB
Cellular Location
Plasma membrane
Myelin membrane
Note: Cytoplasmic side of myelin.
Isoform 3:
Nucleus
Note: Targeted to nucleus in oligodendrocytes.
Involvement in disease
The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS), and fulminating MS (Marburg disease).
PTM
Several charge isomers of MBP; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-B (the least cationic form); are produced as a result of optional PTM, such as phosphorylation, deamidation of glutamine or asparagine, arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H) standing for higher and (L) for lower molecular weight. C3, C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases during aging, making the protein more cationic.
The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6).
Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.
Proteolytically cleaved in B cell lysosomes by cathepsin CTSG which degrades the major immunogenic MBP epitope and prevents the activation of MBP-specific autoreactive T cells.
Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.
More Infomation

Sarmah, R. J., & Kundu, S. (2023). Stable layers of pure myelin basic protein (MBP): Structure, morphology and hysteresis behaviors. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 662, 130973.

Martinsen, V., & Kursula, P. (2022). Multiple sclerosis and myelin basic protein: Insights into protein disorder and disease. Amino Acids, 54(1), 99-109.

Yan, Z., Chu, L., Jia, X., Lin, L., & Cheng, S. (2021). Myelin basic protein enhances axonal regeneration from neural progenitor cells. Cell & Bioscience, 11(1), 1-13.

Smirnova, E. V., Rakitina, T. V., Ziganshin, R. H., Arapidi, G. P., Saratov, G. A., Kudriaeva, A. A., & Belogurov, A. A. (2021). Comprehensive atlas of the myelin basic protein interaction landscape. Biomolecules, 11(11), 1628.

Widder, K., Harauz, G., & Hinderberger, D. (2020). Myelin basic protein (MBP) charge variants show different sphingomyelin-mediated interactions with myelin-like lipid monolayers. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1862(2), 183077.

Träger, J., Widder, K., Kerth, A., Harauz, G., & Hinderberger, D. (2020). Effect of cholesterol and myelin basic protein (MBP) content on lipid monolayers mimicking the cytoplasmic membrane of myelin. Cells, 9(3), 529.

Wąsik, N., Sokół, B., Hołysz, M., Mańko, W., Juszkat, R., Jagodziński, P. P., & Jankowski, R. (2020). Serum myelin basic protein as a marker of brain injury in aneurysmal subarachnoid haemorrhage. Acta Neurochirurgica, 162, 545-552.

Soustelle, L., Antal, M. C., Lamy, J., Rousseau, F., Armspach, J. P., & Loureiro de Sousa, P. (2019). Correlations of quantitative MRI metrics with myelin basic protein (MBP) staining in a murine model of demyelination. NMR in Biomedicine, 32(9), e4116.

Schumacher, H., Wenke, N. K., Kreye, J., Höltje, M., Marcus, K., May, C., & Prüss, H. (2019). IgA autoantibodies against native myelin basic protein in a patient with MS. Neurology-Neuroimmunology Neuroinflammation, 6(4).

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For research use only. Not intended for any clinical use.

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