- Peptide (C)RYLRWDASTRSDLS, corresponding to amino acid residues 39-52 of rat Nrxn3α (Accession Q07310). Extracellular, N-terminus.
- Western blot analysis of mouse brain (lanes 1 and 5), rat brain (lanes 2 and 6), human brain neuroblastoma (SH-SY5Y) cells (lanes 3 and 7) and rat Pheochromocytoma (PC-12) cells (lanes 4 and 8):1-4. Anti-Neurexin 3α (extracellular) Antibody (#ANR-033), (1:200).
5-8. Anti-Neurexin 3α (extracellular) Antibody, preincubated with Neurexin 3α (extracellular) Blocking Peptide (#BLP-NR033).
- Expression of Neurexin 3α in rat and mouse brainImmunohistochemical staining of rat entorhinal cortex (A) and mouse striatum and lateral septum (B) using Anti-Neurexin 3α (extracellular) Antibody (#ANR-033), (1:400). A. Nrxn3α staining (green) appears in neuronal outlines in entorhinal cortex (arrow). B. Nrxn3α staining appeared in axonal processes in striatum (horizontal arrow) and in neuronal cell bodies in lateral septum (vertical arrows). DAPI is used as the counterstain (blue).
Neurexins (NRXNs) are a family of transmembrane, synaptic adhesion molecules. NRXNS were identified as receptors for α-latrotoxin, a presynaptic toxin that triggers massive neurotransmitter release1. Neurexins are largely presynaptic proteins that form a trans-synaptic cell-adhesion complex with postsynaptic neuroligins2. They are encoded by three genes (NRXN1, NRXN2 and NRXN3), each using an upstream promoter to produce the longer α-isoform (α-NRXNs) and a downstream promoter to generate a shorter β-isoform (β-NRXNs).
The α-isoforms and β-isoforms of each neurexin are single-pass transmembrane proteins maintaining identical transmembrane and intracellular domains but having distinct extracellular domains. NRXNs in neurons localize to the presynaptic membrane and bind trans-synaptically to postsynaptic adhesion molecules and receptors3. Neurexins are expressed in all neurons, and are subject to extensive alternative splicing, generating >1,000 splice variants, some of which exhibit highly regulated developmental and spatial expression patterns4.
The structure of α-Neurexins is composed of 6 LNS domains (laminin, neurexin, sex-hormone-binding protein domain) and 3 EGF-like domains. In the mammalian brain they are known to interact with neuroligins, dystroglycan and neurexophilins. Neurexin 3α splicing can give rise to secreted and transmembrane forms of the protein. The biological function of the secreted form remains unknown5.
Changes in Neurexin 3α are associated with autism, drug addiction and obesity6.
Species reactivity key:
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of rat Neurexin 3α. Anti-Neurexin 3α (extracellular) Antibody (#ANR-033) can be used in western blot and immunohistochemistry applications. The antibody recognizes an extracellular epitope and is therefore, highly suited to recognize Nrxn3α in living cells. It has been designed to recognize Nrxn3α from rat, mouse and human samples.
- Anti-Caspr2 Antibody (#APZ-005)
- Anti-CD56/NCAM1 (extracellular)-ATTO Fluor-488 Antibody (#ANR-041-AG)
- Anti-LRRTM1 (extracellular) Antibody (#ANR-141)
- Anti-Neurexin 1α (extracellular) Antibody (#ANR-031)
- Anti-Neurexin 1α (extracellular)-ATTO Fluor-488 Antibody (#ANR-031-AG)
- Anti-Neuroligin 1 (extracellular) Antibody (#ANR-035)
- Anti-Neuroligin 2 (extracellular) Antibody (#ANR-036)
- Anti-Neuroligin 3 (extracellular) Antibody (#ANR-037)