|Catalogue No.||Target||Research Areas||Applications||Size||Price (£)|
|MBP12-100UG||Myelin Basic Protein
Myelin Basic Protein (MBP) is involved in the process of myelination of nerves in the nervous system. MBP Clone 12 recognizes an epitope in the 82-87 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP.
Form in stock: IgG, purified – 1.0 mg/mL. Also available as unpurified supernatant.
Specificity: Reacts with human MBP, recognizing epitopes in the 82-87 amino acid region (DENPVV).
Fusion partner: Spleen cells from an immunised outbred rat were fused with cells of the mouse NS0 myeloma cell line .
Storage: Store at +4°C or -20°C. Avoid repeated freezing and thawing.
Shelf life: 18 months from date of dispatch.
Regulatory/ Restrictions: For research and commercial purposes.
- Van der Goesa, Annette, et al. (2000) The Role of Anti-Myelin (Auto)-Antibodies in the Phagocytosis of Myelin by Macrophages. Journal of Neuroimmunology, 101, 61-67.
- Matsuo, A., Lee, G. C., Terai, K., Takami, K., Hickey, W. F., McGeer, E. G., & McGeer, P. L. (1997). Unmasking of an unusual myelin basic protein epitope during the process of myelin degeneration in humans: a potential mechanism for the generation of autoantigens. The American Journal of Pathology, 150(4), 1253–1266.
- Ioannidou, K., Anderson, K. I., Strachan, D., Edgar, J. M., & Barnett, S. C. (2012). Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo. PLoS ONE, 7(1), e30775.
- Müller, C., Hochhaus, N. M., Fontana, X., Luhmann, H. J., & White, R. (2015). SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis. PLoS ONE, 10(8), e0136900.
- Grigoletto, J., Pukaß, K., Gamliel, A., Davidi, D., Katz-Brull, R., Richter-Landsberg, C., & Sharon, R. (2017). Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss. Acta Neuropathologica Communications, 5, 37.
- Groome NP, Dawkes A, Gales M, Hruby S, Alvord EC Jr. Region-specific immunoassays for human myelin basic protein J Neuroimmunol. 1986 Oct;12(4):253-64. ELISA
- Glynn, P., Chantry, A., Groome, N. and Cuzner, M. L. (1987), Basic Protein Dissociating from Myelin Membranes at Physiological Ionic Strength and pH Is Cleaved into Three Major Fragments. Journal of Neurochemistry, 48: 752–759. WB
- Nigel Groome, Adrian Dawkes, Richard Barry, Sarka Hruby, Ellsworth Alvord Jr., New monoclonal antibodies reactive with defined sequential epitopes in human myelin basic protein, Journal of Neuroimmunology, Volume 19, Issue 4, October 1988, Pages 305-315, ISSN 0165-5728. ELISA
- Maike Friess, Jens Hammann, Petr Unichenko, Heiko J. Luhmann, Robin White, Sergei Kirischuk, Intracellular ion signaling influences myelin basic protein synthesis in oligodendrocyte precursor cells, Cell Calcium, Volume 60, Issue 5, 2016, Pages 322-330, ISSN 0143-4160. WB, Dilution used 1:500
- Sarka Hruby, Ellsworth C. Alvord, Nigel P. Groome, Adrian Dawkes, Russell E. Martenson, Monoclonal antibodies reactive with myelin basic protein, Molecular Immunology, Volume 24, Issue 12, 1987, Pages 1359-1364, ISSN 0161-5890. ELISA
- Homchaudhuri, Lopamudra, Eugenia Polverini, Wen Gao, George Harauz, and Joan M. Boggs. “Influence of Membrane Surface Charge and Post-Translational Modifications to Myelin Basic Protein on Its Ability To Tether the Fyn-SH3 Domain to a Membrane in Vitro.” Biochemistry 48.11 (2009): 2385-393. IF, Dilution used 1:800
- Pohl, Hartmut B. F., Cristina Porcheri, Thomas Mueggler, Lukas C. Bachmann, Gianvito Martino, Dieter Riethmacher, Robin J. M. Franklin, Markus Rudin, and Ueli Suter. “Genetically Induced Adult Oligodendrocyte Cell Death Is Associated with Poor Myelin Clearance, Reduced Remyelination, and Axonal Damage.” Neurobiology of Disease 31.3 (2011): 1069-080. IF, Dilution used 1:300
- Relucio, J., Tzvetanova, I. D., Ao, W., Lindquist, S., & Colognato, H. (2009). Laminin alters Fyn regulatory mechanisms and promotes oligodendrocyte development. The Journal of Neuroscience : The Official Journal of the Society for Neuroscience, 29(38), 11794–11806. ICC
- Savvaki, M., K. Theodorakis, L. Zoupi, A. Stamatakis, S. Tivodar, K. Kyriacou, F. Stylianopoulou, and D. Karagogeos. “The Expression of TAG-1 in Glial Cells Is Sufficient for the Formation of the Juxtaparanodal Complex and the Phenotypic Rescue of Tag-1 Homozygous Mutants in the CNS.” Journal of Neuroscience 30.42 (2010): 13943-3954. WB, Dilution used 1:2000
- Monk, K. R., Oshima, K., Jörs, S., Heller, S., & Talbot, W. S. (2011). Gpr126 is essential for peripheral nerve development and myelination in mammals. Development (Cambridge, England), 138(13), 2673–2680. IHC, Dilution used 1:10
- Brügger, V., Engler, S., Pereira, J. A., Ruff, S., Horn, M., Welzl, H., Jacob, C. (2015). HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins. PLoS Biology, 13(9), e1002258. WB and IF, Dilutions used 1:500 and 1:50 respectively
- Natrajan, M. S., de la Fuente, A. G., Crawford, A. H., Linehan, E., Nuñez, V., Johnson, K. R., … Franklin, R. J. M. (2015). Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination. Brain, 138(12), 3581–3597. ICC, Dilution used 1:500
- Alinda R. Fernandes, Divya M. Chari, Part II: Functional delivery of a neurotherapeutic gene to neural stem cells using minicircle DNA and nanoparticles: Translational advantages for regenerative neurology, Journal of Controlled Release, Volume 238, 2016, Pages 300-310, ISSN 0168-3659. ICC, Dilution used 1:200
- Crawford, A. H., Tripathi, R. B., Foerster, S., McKenzie, I., Kougioumtzidou, E., Grist, M., … Franklin, R. J. M. (2016). Pre-Existing Mature Oligodendrocytes Do Not Contribute to Remyelination following Toxin-Induced Spinal Cord Demyelination. The American Journal of Pathology, 186(3), 511–516. ICC, Dilution used 1:400
- Lim, J. L., van der Pol, S. M. A., Baron, W., McCord, J. M., de Vries, H. E., & van Horssen, J. (2016). Protandim Protects Oligodendrocytes against an Oxidative Insult. Antioxidants, 5(3), 30. ICC, Dilution used 1:200
- Miho Isoda, Jun Kohyama, Akio Iwanami, Tsukasa Sanosaka, Keiko Sugai, Ryo Yamaguchi, Takuya Matsumoto, Masaya Nakamura, Hideyuki Okano, Robust production of human neural cells by establishing neuroepithelial-like stem cells from peripheral blood mononuclear cell-derived feeder-free iPSCs under xeno-free conditions, Neuroscience Research, Volume 110, 2016, Pages 18-28, ISSN 0168-0102. ICC, Dilution used 1:1000
- Kawai, K., Itoh, T., Itoh, A., Horiuchi, M., Wakayama, K., Bannerman, P., … Lindsten, T. (2009). Maintenance of the relative proportion of oligodendrocytes to axons even in the absence of BAX and BAK. The European Journal of Neuroscience, 30(11), 2030–2041. IHC, Dilution used 1:20
- Horiuchi, M., Maezawa, I., Itoh, A., Wakayama, K., Jin, L.-W., Itoh, T., & DeCarli, C. (2012). Amyloid β1–42 oligomer inhibits myelin sheet formation in vitro. Neurobiology of Aging, 33(3), 499–509. WB and ICC, Dilutions used 1:100 and 1:5 respectively
- Pusic, A. D., Pusic, K. M., Clayton, B. L. L., & Kraig, R. P. (2014). IFNγ-stimulated Dendritic Cell Exosomes as a Potential Therapeutic for Remyelination. Journal of Neuroimmunology, 266(0), 12–23. WB, Dilution used 1:1000
- Mitchell L. Meade, Andrea Hoffmann, Meghan K. Makley, Thomas H. Snider, John J. Schlager, Jeffery M. Gearhart, Quantitative proteomic analysis of the brainstem following lethal sarin exposure, Brain Research, Volume 1611, 22 June 2015, Pages 101-113, ISSN 0006-8993. WB, Dilution used 1:1000
Clone MBP12 used to detect mouse myelin binding via Flow Cytometry
Incubation of mouse myelin with mAb against myelin components. The binding is visualized by incubating the mAb-myelin with fluorescent labelled conjugates. The fluorescence intensity (FL2) of the myelin was measured using FACScan flow Cytometry. The data are presented as the geo-mean of fluorescence of one representative experiment (n=4). (Van der Goesa, et al.)
Dilution used: 75μg/ml
Clone MBP 12 used to detect myelinated structures in MS plaques by IHC-P
Serial sections of paraffin-embedded MS tissue immunostained with anti-EP(A), clone26(B), clone2(C), clone14(D), clone12(E), or clone22(F) .Notice that only abnormal myelin tissues strongly stained by anti-EP, whereas all other antibodies strongly stain the normal myelin surrounding the plaque area. See Materials and Methods for details. (Matsuo, A et al.)
Dilution used: 1:100,000
Clone 12 used to detect MBP in myelinating cell cultures using Immunofluorescence
Immunohistochemistry of transplanted neurospheres demonstrate that cyto-GFP labelled cells form early and mature myelinating oligodendrocytes.
Cyto-GFP-expressing neurospheres were transplanted into a shiverer mouse 3, 7 or 15 days post-transplantation, and 10 µm thick frozen sections were cut and immunolabelled with antibodies to GFP and MBP (Ioannidou, K et al.)
Dilution used: 1:500
Clone 12 used to detect expression of MBP in mouse brain lysates via Western Blot and ICC
A. MBP protein can only be detected by immunocytochemistry in differentiated Schwann cells B, Western Blots of undifferentiated and differentiated primary Schwann cells show MBP protein only present in differentiated Schwann cells
C, MBP and sncRNA715-specific RT-PCR on RNA extracted from undifferentiated or differentiated primary Schwann cells (Müller, C et al.)
Dilution used: 1:50 (ICC) 1:500 (WB)
Clone 12 used to detect MBP in mouse oligodendrocytes using Immunofluorescence and Western Blot
α-Syn impairs oligodendrocyte maturation. Oligodendrocyte progenitor cells were either untreated (Co) or incubated with rh α-Syn (10 μg/ml) 2 h after plating for 3 or 6 days. Cells were subjected to immunocytochemistry using antibodies: a anti-acetylated α-tubulin (green) and anti-MBP (red); b anti-proteoglycan NG-2 (green) and anti-MBP (red). Nuclei were stained with DAPI (blue). Scale bar: 20 μm. c Exogenously applied α-Syn led to an increase in NG-2 and a decrease in MBP levels. (Grigoletto, J et al.)
Dilution used: 1:1500 (WB) 1:200 (ICC)