|Related Categories||1-1B, Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Neural Stem Cells,|
|species reactivity||canine, pig, sheep, human, mouse, bovine, rat, rabbit|
|does not react with||guinea pig, chicken|
|application(s)||immunohistochemistry: suitable using brain sections|
|indirect ELISA: suitable|
|western blot: 1:500 using fresh bovine brain extract|
|antibody form||ascites fluid|
|contains||15 mM sodium azide|
|shipped in||dry ice|
human ... CNP(1267)|
mouse ... Cnp(12799)
rat ... Cnp(25275)
human 2′,3′-cyclic nucleotide-3′-phosphodies
CNPase (2′,3′-cyclic nucleotide 3′-phosphodiesterase, E.C.3.1.4. 37) is a unique enzyme. It is a constituent of cells that elaborate myelin in the central and peripheral nervous systems, i.e. oligodendrocytes and Schwann cells respectively, and is virtually absent in other cell types in the nervous system.
The enzyme isolated from mammalian brain is primarily a mixed dimer of approximately 94 kDa. The dimer consists of a varied proportion of CNP1 (46 kDa) and CNP2 (48 kDa) subunits in various species. The high levels of CNPase observed in oligodendrocytes and Schwann cells portend a vital role of this enzyme in the normal function of these cells. They are distinguished from nearly all other cells by their ability to synthesize and maintain vast amounts of multilamellar membrane, known as myelin. It seems very likely that CNPase is expressed at high levels in these particular cells to facilitate the elaboration and maintenance of myelin or to carry out functions imposed or afforded by the unique membrane structure of myelin. 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 immunodefi ciency with CNS involvement, peripheral neuropathies, etc. Another important use is the study of reinnervation of the neuromuscular junction and the identification of oligodendrocyte progenitor cells, very early in postnatal development.
Monoclonal Anti-CNPase reacts specifically with CNPase in ELISA, immunoblotting and immunohistochemical staining of brain sections. In an immunoblotting assay, the antibody localizes both CNP1 (46kD) and CNP2 (48kD) bands of the enzyme and recognizes whole brain CNPase of human, bovine, mouse, rat, rabbit, dog, sheep and pig but not guinea pig or chicken. Immunohistochemical staining performed on paraffin, cryostat, or vibratome sections of rat brain, reveals a selective staining of oligodendrocytes in the grey and white matter. Nerve cells and axons are not stained and astroglial cells do not appear to be labeled.
The antibody reacts specifically with CNPase in oligodendrocytes and Schwann cells. Recognizes whole brain CNPase. Nerve cells, axons, and astroglial cells do not appear to be labeled. Using immunoblotting techniques, the antibody localizes both CNP1 and CNP2 bands of the enzyme.
Monoclonal Anti-CNPase may be used for the localization of CNPase using various immunochemical assays such as ELISA, immunoblot, dot blot and immunocytochemistry.
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Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
Monoclonal antibody production to human and bovine 2':3'-cyclic nucleotide 3'-phosphodiesterase (CNPase): high-specificity recognition in whole brain acetone powders and conservation of sequence between CNP1 and CNP2. Brain Res. Sprinkle, T.J, et al. Brain Res. 426, 349-357, (1987)
The neuroblast and angioblast chemotaxic factor SDF-1 (CXCL12) expression is briefly up regulated by reactive astrocytes in brain following neonatal hypoxic-ischemic injury Walker, A.L., et al. BMC Neurosci. 6, 63, (2005)
Combined extrinsic and intrinsic manipulations exert complementary neuronal enrichment in embryonic rat neural precursor cultures: an in vitro and in vivo analysis. Furmanski, O., et al Comparative Neurology 515, 56-71, (2009)
Reduced immunoproteasome formation and accumulation of immunoproteasomal precursors in the brains of lymphocytic choriomeningitis virus-infected mice. Kremer, M., et al. J. Immunol. 185, 5549-60, (2010)
Molecular and morphological configuration for 2-arachidonoylglycerol-mediated retrograde signaling at mossy cell-granule cell synapses in the dentate gyrus. Uchigashima, M., et al. J. Neurosci. 31, 7700-14, (2011)
Human stem/progenitor cells from bone marrow enhance glial differentiation of rat neural stem cells: a role for transforming growth factor β and Notch signaling. Robinson, A.P., et al. Stem Cells Dev. 20, 289-300, (2011)
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