High CNPase expression is seen in myelin producing cells, including oligodendrocytes and Schwann cells. CNPase accounts for roughly 4% of the total myelin protein in the central nervous system (CNS). CNPase binds to tubulin heterodimers and plays a role in tubulin polymerization, and oligodendrocyte process outgrowth. The enzyme isolated from the mammalian brain is primarily a mixed dimer of approximately 94 kD. The dimer consists of a varied proportion of CNP1 (46 kD) and CNP2 (48 kD) subunits in various species. Since the enzyme is a myelin-associated enzyme, it is of considerable interest in the study of diseases and disorders in which myelin is affected, such as multiple sclerosis, subacute sclerosing panencephalitis, acquired immunodeficiency with CNS involvement, and peripheral neuropathies. The combination of clone SMI 91 with clone SMI 94 and/or clone SMI 99 is useful for immunocytochemical studies on the progression of normal and pathologic myelination.
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