C5922
Monoclonal Anti-CNPase antibody produced in mouse
clone 11-5B, ascites fluid
Synonym(s):
Anti-CNP1, Anti-HLD20
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
11-5B, monoclonal
contains
15 mM sodium azide
species reactivity
mouse, rat, bovine, canine, pig, human, rabbit, sheep
should not react with
guinea pig, chicken
technique(s)
immunohistochemistry: suitable using brain sections
indirect ELISA: suitable
microarray: suitable
western blot: 1:500 using fresh bovine brain extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CNP(1267)
mouse ... Cnp(12799)
rat ... Cnp(25275)
Related Categories
General description
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.
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.
Specificity
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.
Immunogen
human 2′,3′-cyclic nucleotide-3′-phosphodiesterase (E.C.3.1.4.37, CNPase).
Application
Monoclonal Anti-CNPase may be used for the localization of CNPase using various immunochemical assays such as ELISA, immunoblot, dot blot and immunocytochemistry. It has also been used in immunohistochemistry.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
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Oligodendrocytes are damaged by neuromyelitis optica immunoglobulin G via astrocyte injury
Marignier R, et al.
Brain, 133(9), 2578-2591 (2010)
Deficiency of schnurri-2, an MHC enhancer binding protein, induces mild chronic inflammation in the brain and confers molecular, neuronal, and behavioral phenotypes related to schizophrenia
Takao K, et al.
Neuropsychopharmacology, 38(8), 1409-1409 (2013)
Fulminant JC virus encephalopathy with productive infection of cortical pyramidal neurons
Wuthrich C, et al.
Annals of Neurology, 65(6), 742-748 (2009)
Natalia D Andersen et al.
Scientific reports, 6, 31781-31781 (2016-08-24)
We herein developed a protocol for the rapid procurement of adult nerve-derived Schwann cells (SCs) that was optimized to implement an immediate enzymatic dissociation of fresh nerve tissue while maintaining high cell viability, improving yields and minimizing fibroblast and myelin
Kadiombo Bantubungi et al.
Molecular and cellular neurosciences, 37(3), 454-470 (2007-12-18)
Neural and mesenchymal stem cells have been proposed as alternative sources of cells for transplantation into the brain in neurodegenerative disorders. However, the endogenous factors controlling their engraftment within the injured parenchyma remain ill-defined. Here, we demonstrate significant engraftment of
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