|Detection of Neuropilin‑2 in C6 Rat Cell Line by Flow Cytometry. C6 rat glioma cell line was stained with Mouse Anti-Rat Neuropilin‑2 Alexa Fluor® 488‑conjugated Monoclonal Antibody (Catalog # FAB567G, filled histogram) or isotype control antibody (Catalog # IC0041G, open histogram). View our protocol for Staining Membrane-associated Proteins.|
Neuropilin-2 (Npn-2), previously known as Npn-1-related molecule, is a 120-140 kDa type I transmembrane protein that belongs to the neuropilin family of molecules. It binds members of the class III secreted semaphorin subfamily (Sema3C and 3F), multiple VEGFs (VEGF145, VEGF165, VEGF-C and VEGF-D), PlGF, and HGF, and forms complexes with NRP1, Plexin A1,A2, A3, A4 and Plexin B1, plus VEGFR1, 2 and 3, and Integrin alpha 6 beta 1. The extracellular domain of these proteins is composed of two N-terminal CUB (complement-binding) domains (domains a1 and a2), two domains with homology to coagulation factors V and VIII (domains b1 and b2) and a MAM (meprin) domain (domain c). In the absence of ligands, neuropilins can form homo- and hetero-oligomers via homophilic interactions of their MAM domains. At the amino acid (aa) sequence level, Npn-2 shares 96% and 94% aa sequence identity with mouse and human Neuropilin-2, respectively. The expression patterns of Npn-1 and Npn-2 in developing neurons of the central and peripheral nervous systems are largely, though not completely non-overlapping. Npn-2 is expressed by vascular and lymphatic endothelim plus tumor cells, and has been suggested to appear also on macrophages, GABAergic neurons and proximal convoluted tubule cells.
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