Technical Data
Myelin Basic Protein, aa82-87 (MBP)
Myelin basic protein (MBP) is a single-chain, flexible polypeptide of about 18.5kD existing in its natural environment as an extrinsic and loosely bound component of the cytoplasmic portion of the myelin membrane sandwich. Ultrastructural immunocytochemistry with anti-myelin basic protein has shown that MBP is localized in the compact myelin sheath. MBP has not been demonstrated in rough endoplasmic reticulum, lysosomes or any other cytoplasmic organelles (3). MBP serves as a marker for oligodendrocytes and Schwann cells (3). MBP is also a marker for malignant schwannomas (4) and appears to play a significant role in the etiology of multiple sclerosis (5-7) and experimental autoimmune encephalomyelitis (8).

Suitable for use in Western Blot, ELISA, RIA and Immunohistochemistry. Other applicaitons have not been tested.

Recommended Dilution:
Immunohistochemistry: Frozen sections

Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
1ml4°C (-20°C Glycerol)Blue IceBovineRat
Not determined
Bovine myelin basic protein.
Supplied as a liquid, supernatant, 0.09% sodium azide.
Reacts with intact MBP and synthetic peptide aa82-99. Reacts weakly with peptides ending in the phe 91 where the 91-92 phe-phe bond is broken. Epitope: Mapped to the region DENPVV. Species crossreactivity: Human bovine, sheep, rabbit, mouse and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Groome, N.P., et al., J. Neuroimmunol. (1986) 12:253-264. 2. Martenson, R.E. (1984) in Experimental Allergic Encephalomyelitis. A useful model for Multiple Sclerosis (Alvord, Kies and Suckling eds) pp 511-521. Alan Liss N.Y. 3. Glynn, P., et al., J. Neurochem (1987) 48:752-759. 4. Hruby, S., et al., Molecular Immunology In press. 4. Day, E.D. and Potter, N.T (1986) J. Neuroimmunol. 10, 289. 5. Hashim, G.A. (1978) Immunol. Rev. 39, 60. 6. Golo, M. (1987) Histochemistry 87, 201. 7. Mogollon, R., et al. (1984) Cancer 53, 1190. 7. Whitaker, J.N. (1984) Ann. N.Y. Acad. Sci. 436, 140. 9. Eidinoff, H. (1988) Med. Hypotheses 26, 103. 10. tar Meulen, V. (1988) Ann. N.Y. Acad. Sci. 540, 202. 11. Kerlero de Rosbo, N., et al. (1985) J. Neuroimmunol. 9, 349. 12. Sires, L.R., et al. (1981) Science 214, 87.