• Nature
  • Source
  • Amino Acid Sequence
    • Accession
    • Sequence
      aaqkrpsqrs kylasastmd harhgflprh rdtgildslg rffgsdrgap krgsgkdghh aartthygsl pqkaqghrpq denpvvhffk nivtprtppp sqgkgrglsl srfswgaegq kpgfgyggra sdyksahkgl kghdaqgtls kifklggrds rsgspmarr
    • Molecular weight
      18 kDa
    • Amino acids
      1 to 169
  • Conjugation


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.

  • Biological activity

    Acting as substrate of MAP Kinase such as ERK1 and ERK2

  • Form
  • Additional notes
    Myelin 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

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Constituent: 2.09% MOPS

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • GDB
    • Golli MBP
    • Golli MBP; myelin basic protein
    • Hemopoietic MBP
    • HMBPR
    • HUGO
    • MBP
    • MGC99675
    • MLD
    • Myelin A1 protein
    • Myelin A1 Protein, basic
    • Myelin basic protein
    • Myelin Deficient
    • Myelin membrane encephalitogenic protein
    • OTTHUMP00000163776
    • OTTHUMP00000174387
    • OTTHUMP00000174388
    • SHI
    • Shiverer
    • SP
    see all
  • 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.
  • Tissue specificity
    MBP 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 disease
    Note=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 similarities
    Belongs to the myelin basic protein family.
  • Developmental stage
    Expression 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.
  • Post-translational
    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.
  • Cellular localization
    Myelin membrane. Cytoplasmic side of myelin.
  • Information by UniProt


  • 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


This product has been referenced in:
  • Fauster A  et al. A cellular screen identifies ponatinib and pazopanib as inhibitors of necroptosis. Cell Death Dis 6:e1767 (2015). Read more (PubMed: 25996294) »
See 1 Publication for this product

Customer reviews and Q&As


Thank you for your enquiry. The molecular ratio for biotin:MBP is approximately 3:1. I hope this information helps. Please do not hesitate to contact us if you need anything further.

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