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Rat Anti-MBP Recombinant Antibody (12) (CBMAB-1602-CN)

This product is a rat antibody that recognizes MBP of bovine. The antibody 12 can be used for immunoassay techniques such as: ELISA, FC, IF, IHC-Fr, IHC-P, WB.
See all MBP antibodies
Published Data
Fig.1 Western blotting of myelin proteins MBP and CNP.
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Fig.2 Immunohistochemistry of MBP and axonal marker SMI312 in the ventral medial white matter at P8.
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Summary

Host Animal
Rat
Specificity
Cattle, Mouse, Rat, Sheep, Rabbit, Goat, Human
Clone
12
Antibody Isotype
IgG2a
Application
ELISA, FC, IF, IHC-Fr, IHC-P, WB

Basic Information

Immunogen
Full length protein (Cow)
Specificity
Cattle, Mouse, Rat, Sheep, Rabbit, Goat, Human
Antibody Isotype
IgG2a
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
Tissue culture supernatant
Preservative
0.1% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
Localized in aa. 82-87 (DENPVV)

Target

Full Name
MAP3K12 Binding Inhibitory Protein 1
Introduction
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. 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.
Entrez Gene ID
Human4155
Mouse17196
Rat24547
Goat106503529
Rabbit100344447
Sheep101109407
Cattle618684
UniProt ID
HumanP02686
MouseP04370
RatP02688
GoatA0A452DL22
RabbitP25274
SheepW5P2N0
CattleP02687
Alternative Names
myelin basic protein; 20 kDa microtubule-stabilizing protein; microtubule-stabilizing protein; myelin A1 protein
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.

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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