Neurexins are a family of neuron-specific cell surface proteins that contain hundreds of isoforms. These isoforms are generated from two different promoters in three different genes that code for many splice-variant transcripts. In rat, neurexins include 160-200 kDa α-neurexins and 90-100 kDa β-neurexins, which include multipe isoforms identified as neurexin I, II, or III. Full-length α-neurexins contain three repeating domains that include a left arm (A) cell interaction module (LNS), a central EGF domain, and a right arm (B) LNS. β-neurexins are identical to α-neurexins in the C-terminal region, but lack the five LNS repeats and three EGF domains of α -neurexins. Neurexin Iα was first characterized as a Ca2+-dependent receptor for α-latrotoxin, the excitatory neurotoxin in black widow spider venom. The C-terminus of Neurexin Iα interacts with the synaptic vesicle protein, synaptotagmin, while the three repeated sequences in the extracellular region have homology to cell adhesion-related proteins. Thus, Neurexin Iα may be important for cell-cell interactions and synaptic protein localization during the neuronal differentiation.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.