Neuropilin-1 (NRP1)

NRP1 is a transmembrane receptor that is involved in numerous biological processes, including angiogenesis, vascular permeability, axon guidance, and mitochondrial iron transport. In October 2020, NRP1 was first demonstrated to facilitate SARS-CoV-2 entry (J. L. Daly et al., Science 10.1126/science.abd3072 (2020)). After the SARS-CoV-2 Spike protein binds to the endogenous ACE2 receptor, the Spike protein is cleaved into two polypeptides: S1 and S2. The C-end rule motif on the S1 polypeptide binds to NRP1. Inhibition of this interaction reduces viral entry.

Neuropilin-1 domains
Figure 1. Human NRP1 protein domains. There are two isoforms of human NRP1 proteins: the large isoform 1 (Product 230-30178) and the small one (Product 230-30176). Both NRP1 isoforms have b1b2 domains binding to SARS-CoV-2 S1 subunit CendR domains (Product 230-30179, 230-30180). The numbers below the domains show the amino acid position.

Recombinant Human NRP1 Protein

Catalog # Species Protein Domain Purification Expression Host Expression Region Tag MW (kDa)
230-30176 Human Isoform 2, full length Purified HEK293 Cell Phe22-Lys644 C-terminal His-tag ∼90 kDa
230-30178 Human Isoform 1, full length Purified HEK293 Cell Phe22-Pro856 C-terminal His-tag ∼120 kDa

References

  • Ludovico Cantuti-Castelvetri, et al. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity. Science. 370, 856–860 (2020).
  • James L. Daly, et al. Neuropilin-1 is a host factor for SARS-CoV-2 infection. Science. 370, 861-865 (2020).