Active Myelin Basic Protein full length protein (ab792)
- Product nameActive Myelin Basic Protein full length proteinSee all Myelin Basic Protein proteins and peptides ...
- DescriptionRecombinant, Biotin
Our Abpromise guarantee covers the use of ab792 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Additional NotesMyelin basic protein (MBP) is isolated from bovine brain. It is well documented that MBP is a substrate for many protein kinases including PKC, PKA, and MAPK family (such as ERK1/2). Biotinylated MBP is an excellent substrate for the solid-phase kinase assay system, facilitating the separation of free ATP and the kinases. Biotinylated MBP could enhance the efficiency of immobilization of the substrate on an avidin-coated microplate and the substrate will be readily accessible for the kinase activity through a large molecule avidin as a spacer. We do not sell non-biotinylated MBP.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 0.1M MOP. pH 4.0-4.5
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Golli MBP
- Golli MBP; myelin basic protein
- Hemopoietic MBP
- Myelin A1 Protein
- Myelin basic protein
- Myelin Deficient
- Myelin Membrane Encephalitogenic Protein
- FunctionThe 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.
- Tissue specificityMBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system.
- Involvement in diseaseNote=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).
- Sequence similaritiesBelongs to the myelin basic protein family.
- Developmental stageExpression begins abruptly in 14-16 week old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. Isoform 4 expression is more evident at 16 weeks and its relative proportion declines thereafter.
modificationsSeveral 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.
- Cellular localizationMyelin membrane. Cytoplasmic side of myelin.
Active Myelin Basic Protein full length protein images
MBP and Biotinylated MBP was phosphorylated with 0.05ug of active ERK1 with P32 radiolabeled ATP.
Assay reference: Sanghera JS et al., J Immunol. (1996) 156:4457-4465
Activity of biotinylated MBP
Lane a (5 ug of biotinylated MBP): 33682 counts/min
Lane b (2.5 ug of biotinylated MBP): 18478 counts/min
Lane c (1.25 ug of biotinylated MBP): 6714 counts/min
Lane d (0.625 ug of biotinylated MBP): 2889 counts/min
Lane e (0.36 ug of biotinylated MBP): 1039 counts/min
Lane f (0.18 ug of biotinylated MBP): 633 counts/min
Control Lane (0.0 ug of biotinylated MBP): 145 counts/min
Non-biotinylated MBP Activity
Lane A (5 ug of biotinylated MBP): 37604 counts/min
Lane B (2.5 ug of biotinylated MBP): 17824 counts/min
Lane C (1.25 ug of biotinylated MBP): 8867 counts/min
Lane D (0.625 ug of biotinylated MBP): 4190 counts/min
Lane E (0.36 ug of biotinylated MBP): 2248 counts/min
Lane F (0.18 ug of biotinylated MBP): 1500 counts/min
Control Lane (0.0 ug of biotinylated MBP): 218 counts/min
References for Active Myelin Basic Protein full length protein (ab792)
ab792 has not yet been referenced specifically in any publications.