Anti-Neuropilin 1 / NRP1, clone NRP1/4620

1 mg/ml in 1X PBS, BSA free, sodium azide free. Neuropilin is a type I transmembrane receptor that has been implicated in aspects of axon growth and guidance and has been shown to act as a high affinity receptor for class III semaphorins and vascular endothelial growth factor (VEGF). A closely related protein, neuropilin-2, shares a common domain structure and signifcant homology with neuropilin and also acts as a receptor for the class III semaphorins and VEGF. Both neuropilins are involved in regulating many physiological pathways including axonal guidance and angiogenesis, however they exhibit differential expression in the adult vasculature. Neuropilin-2 is polysialylated and expressed on the surface of dendritic cells. It is also expressed by venous and lymphatic endothelium. Neuropilin is expressed predominantly by arterial endothelium. Protein function: Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins (PubMed:9288753, PubMed:9529250, PubMed:10688880). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:9288753, PubMed:9529250, PubMed:10688880, PubMed:19805273). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799). [The UniProt Consortium]