Use at an assay-dependent concentration. For Sandwich ELISA pairing: Human Neuropilin-1 Antibody(Capture) (EPA1882C), with Human Neuropilin-1 Protein (EPA1882S) as assay standards. The reference range value is 976.6-125,000 pg/mL.
Target info
Function
Neuropilin-1 (NRP1, also CD304 or BDCA-4) is a multifunctional single-pass type I transmembrane co-receptor, encoded in humans by the NRP1 gene on chromosome 10p11. It possesses a large extracellular lumen composed of two CUB (a1/a2) domains, two coagulation factor V/VIII homology (b1/b2) domains, and one meprin-like (c) oligomerization domain, followed by a short transmembrane helix and a small cytoplasmic tail of ~40 amino acids that ends in a PDZ-binding motif capable of recruiting the adaptor synectin/GIPC. NRP1 is expressed on endothelial cells (especially arteries during development), neurons and axons, dendritic cells, tumor cells, and regulatory T cells, and localizes to the plasma membrane with some cytoplasmic internalized pool. It is a non-signaling co-receptor that pairs with two distinct receptor classes: (i) vascular endothelial growth factor receptors, principally VEGFR2/KDR, to which it binds the heparin-binding VEGF165 isoform (and VEGFB and PlGF-2) with high affinity, lowering the ligand requirement and amplifying VEGFR2-mediated PI3K/Akt, MAPK/ERK, and FAK signaling that drives endothelial-cell chemotaxis, survival, and developmental and tumor angiogenesis; and (ii) plexin A receptors, to which it presents class 3 semaphorins (especially SEMA3A), converting SEMA3 binding into repulsive axon-guidance signals that pattern neuronal projections and regulate vascular permeability. NRP1 also recognizes a C-end Rule (CendR) R/KXXR/K motif on ligands such as VEGF and the tissue-penetrating peptide iRGD, triggering receptor internalization and vascular leakage. More recently it has been identified as an attachment co-receptor for the SARS-CoV-2 spike protein. Subcellularly, NRP1 is a plasma membrane co-receptor that undergoes ligand-specific clathrin-dependent (VEGF) or lipid-raft-dependent (semaphorin) endocytosis; a truncated cytosolic isoform has also been described.
