Rat Neuropilin‑2 Biotinylated Antibody

Neuropilin-1 (Npn-1, previously known as neuropilin) and Npn-2 (previously known as Npn-1-related molecule) are type I transmembrane proteins that bind members of the class III secreted semaphorin subfamily which are implicated in repulsive axon guidance. 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 sequence level, Npn-1and Npn-2 share 44% identity. Npn-1 and Npn-2 show different binding specificities for different members of the semaphorin family. The expression patterns of Npn-1 and Npn-2 in developing neurons of the central and peripheral nervous systems are largely, though not completely nonoverlapping. Npn‑1 and Npn-2 are also expressed by endothelial and tumor cells and have been shown to be isoform-specific receptors for VEGF₁₆₅. Npn‑1 was also reported to bind PlGF-2 and the VEGF-like protein from of virus NZ2.