Neuropilin-2a Extracellular Domain (human, recombinant)

Neuropilin-2 (NRP-2) is a non-tyrosine kinase transmembrane glycoprotein co-receptor for class III semaphorins and VEGFs.¹ It is composed of two CUB domains (a1 and a2), two Factor V/VIII homology domains (b1 and b2), a MAM domain, a transmembrane region, and a cytoplasmic tail. The a1, a2, and b1 domains are responsible for binding to class III semaphorins, including semaphorin-3C (Sema3C) and Sema3F, the b1 and b2 domains are responsible for binding to VEGFs, including VEGFA₁₆₅, VEGFA₁₄₅, VEGFC, VEGFD, and placenta growth factor (PlGF), and the MAM domain is important for homo- or heterodimerization.^1,2 NRP-2 exists in three main isoforms: membrane-bound NRP-2a and NRP-2b, which are generated by alternative splicing and differ by the presence or absence, respectively, of the PDZ binding motif in the C-terminus, and soluble NRP-2 (sNRP-2), which is composed of the a1, a2, and b1 domains and a partial b2 domain.¹ NRP-2a is expressed in the brain, heart, kidney, liver, lungs, placenta, trachea, and small intestine.³ NRP-2 is a co-receptor for VEGFR2 and VEGFR3 and is involved in angiogenesis, lymphangiogenesis, and neuronal guidance, as well as some immune functions such as T cell migration.^2,4,1 Knockout of Nrp2a induces misprojections of axons originating from olfactory sensory neurons expressing transient receptor potential canonical 2 (TRPC2) in zebrafish.⁴ High tumoral expression of NRP2A is associated with poor overall survival in patients with muscle-invasive bladder cancer.⁵ Cayman’s Neuropilin-2a Extracellular Domain (human, recombinant) protein can be used for ELISA. This protein consists of 844 amino acids, has a calculated molecular weight of 95 kDa, and a predicted N-terminus of Gln23 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 100-110 kDa due to glycosylation.

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1. Roy, S., Bag, A.K., Singh, R.K., et al. Multifaceted role of neuropilins in the immune system: Potential targets for immunotherapy. Front. Immunol. 8, 1228 (2017).

2. Rapisarda, A., and Melillo, G. Role of the VEGF/VEGFR axis in cancer biology and therapy. Advances in cancer research 114, 237-267 (2012).

3. Rossignol, M., Gagnon, M.L., and Klagsbrun, M. Genomic organization of human neuropilin-1 and neuropilin-2 genes: Identification and distribution of splice variants and soluble isoforms. Genomics 70(2), 11-22 (2000).

4. Cheng, R.P., Dang, P.M.C., Taku, A.A., et al. Loss of neuropilin2a/b or sema3fa alters olfactory sensory axon dynamics and protoglomerular targeting. Neural Dev. 17(1), 1 (2022).

5. Förster, S., Givehchi, M., Nitschke, K., et al. Neuropilin-2 and Its transcript variants correlate with clinical outcome in bladder cancer. Genes (Basel) 12(4), 550 (2021).