Human Neuropilin-2 (NRP-2), His-Tag

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Recombinant human Neuropilin-2, His-tag (amino acids 23-864), expressed in HEK293 cells and purified from culture supernatant. The cytoplasmic tail and the transmembrane region have been replaced by a 9 amino acid glycine-serine linker followed by a 6x histidine tag. This recombinant protein has been confirmed to bind (by ELISA) to the human Cytomegalovirus (HCMV) pentameric gH/gL complex, as described by Martinez-Martin et al. The complex is composed of the gH/gL heterodimer bound to a trio of small glycoproteins encoded by UL128, UL130, and UL131 (also known as UL131A).



  • Recombinant human Neuropilin-2 (NCBI accession number NP_957718.1), amino acids 23-864. The cytoplasmic tail and the transmembrane region were replaced by a 9 amino acid glycine-serine linker followed by a 6x histidine tag.
  • Expressed in human embryonic kidney (HEK) 293 cells and purified from culture supernatant.
  • Presented in DPBS, pH7.4



There are two homologs of the NRP family, NRP1 and NRP2, which are 130 kDa single-pass transmembrane glycoproteins that act as non-tyrosine kinase co-receptors. They contain 4 distinct domains including a CUB domain, a FV/FVIII domain, a MAM domain and a domain that contains the transmembrane and short cytoplasmic region. Both homologues can homo- and hetero-multimerize; the encoded transmembrane protein binds to SEMA3C and SEMA3F proteins and interact with vascular endothelial growth factor (VEGF) and PLGF-2 isoform of PGF. NRP-2 is believed to play a role in cardiovascular development, axon guidance and tumorigenesis.

NRP_2 is also a receptor for human Cytomegalovirus pentamer-dependent entry in epithelial and endothelial cells. It was identified using a high-throughput avidity-based extracellular interaction screen (AVEXIS), in which recombinant single-pass transmembrane proteins were observed in vitro for interactions with recombinant trimer and pentamer. Following its identification, NRP-2 was determined to be essential for pentamer-dependent HCMV infection of endothelial and epithelial cells. NRP-2 also directly interacts with Human T-lymphotropic virus-1 (HTLV-1) surface glycoprotein SU, a furin-processed heparin-binding protein, and is essential for HTLV-1 viral entry. Epstein-Barr Virus (EBV) infection of nasopharyngeal epithelial cells is mediated by binding of NRP-1 to the EBV glycoprotein B (gB) protein. However, while gB binds tightly to both proteins, NRP-1 enhances EBV infection while NRP-2 impairs EBV infection.



  • Appleton (2007). Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. EMBO J. 26(23):4902-12.
  • Ellis (2006). The role of neuropilins in cancer. Mol Cancer Ther. 2006 May;5(5):1099-107.
  • Ghez et al. (2006). Neuropilin-1 is involved in human T-cell lymphotropic virus type 1 entry. J Virol. 80(14):6844-54.
  • Guo and Vander Kooi (2015). Neuropilin Functions as an Essential Cell Surface Receptor. J Biol Chem. 290(49):29120-6.
  • Martinez-Martin et al. (2018). An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a Central Viral Receptor. Cell. 2018 Aug 23;174(5):1158-1171.
  • Nakamura and Goshima (2002). Structural and functional relation of neuropilins. Adv Exp Med Biol. 515:55-69.
  • Nguyen and Kamil (2018). Pathogen at the Gates: Human Cytomegalovirus Entry and Cell Tropism. Viruses. 10(12).
  • Lambert (2009). HTLV-1 uses HSPG and neuropilin-1 for entry by molecular mimicry of VEGF165. Blood. 113(21):5176-85.
  • Wang et al. (2015). Neuropilin 1 is an entry factor that promotes EBV infection of nasopharyngeal epithelial cells. Nat Commun. 6:6240.
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