Overview
- Peptide (C)REKKDVPLGPEDPK, corresponding to amino acid residues 1142-1155 of rat NFASC (Accession P97685). Intracellular, C-terminus.
Western blot analysis of rat brain (lanes 1 and 4), mouse brain (lanes 2 and 5) and rat hippocampus (lanes 3 and 6) lysates:1-3. Anti-Neurofascin Antibody (#AIP-025), (1:800).
4-6. Anti-Neurofascin Antibody, preincubated with Neurofascin Blocking Peptide (#BLP-IP025).
Expression of Neurofascin in rat spinal cord.Immunohistochemical staining of perfusion-fixed frozen rat brain sections with Anti-Neurofascin Antibody (#AIP-025), (1:200), followed by goat anti-rabbit-AlexaFluor-488. A. Neurofascin immunoreactivity (green) appears dense in the dorsal horn (DH) and sparse in the dorsal column (DC). B. Pre-incubation of the antibody with Neurofascin Blocking Peptide (BLP-IP025), suppressed staining. Cell nuclei are stained with DAPI (blue).
Expression of Neurofascin in mouse hippocampus.Immunohistochemical staining of perfusion-fixed frozen mouse brain sections with Anti-Neurofascin Antibody (#AIP-025), (1:200), followed by goat anti-rabbit-AlexaFluor-488. A. Staining in the hippocampal dentate gyrus region, showed Neurofascin immunoreactivity (green) in the hilus (H) and in an outside layer (arrows). B. Pre-incubation of the antibody with Neurofascin Blocking Peptide (BLP-IP025), suppressed staining. Cell nuclei are stained with DAPI (blue).
- Volkmer, H. et al. (1992) J. Cell Biol. 118, 149.
- Ratcliffe, C.F. et al. (2001) J. Cell Biol. 154, 427.
- Charles, P. et al. (2002) Cur. Biol. 12, 217.
- Koroll, M. et al. (2001) J. Biol. Chem. 276, 10646.
Neurofascin belongs to the L1 subgroup of the immunoglobulin superfamily of cell adhesion molecules and is an axon associated surface glycoprotein implicated in axonal growth and fasciculation.
Neurofascin is comprised of four structural elements: At the NH2 terminus, neurofascin contains six Ig-like motifs of the C2 subcategory followed by four fibronectin type III (FNIII)-related repeats. Between the FNIII-like repeats and the plasma membrane spanning region, neurofascin contains a 75-amino acid residues rich in proline, alanine and threonine which might be the target of extensive O-linked glycosylation. A transmembrane segment is followed by a 113-amino acid residues-long cytoplasmic domain1.
Neurofascin associates with sodium channel β1 (NaVβ1) units via interaction of its first Ig-like domain and second fibronectin type III–like domain with the extracellular Ig-like domain of β1. NaVβ1 subunits localize to nodes of Ranvier with neurofascin in sciatic nerve axons. NaVβ1 and neurofascin are associated as early as postnatal day 5, during the period that nodes of Ranvier are in formation2.
Unlike L1 and other subgroup members, neurofascin is subjected to extensive alternative splicing that is regulated during embryonic development of the brain. An oligodendroglial isoform of neurofascin, NF155, serves as a glial receptor for the paranodin/Caspr-contactin complex. The extracellular domain of NF155 binds to the complex at the cell surface3.
Anti-Neurofascin Antibody (#AIP-025) is a highly selective antibody directed against an epitope of the rat protein. The antibody can be used in western blot analysis. It has been designed to recognize NFASC from human, mouse, and rat samples.
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