Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

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Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE with silver staining
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Mouse Neuropilin-2 Fc Chimera at 5 μg/mL (100 μL/well) can bind Recombinant Human VEGF165 (Catalog # 293‑VE) in the presence of 2 μg/mL of heparin with an apparent Kd <1nM.
Mouse myeloma cell line, NS0-derived mouse Neuropilin-2 protein
Mouse Neuropilin-2
Accession # O35375
N-terminus C-terminus
Accession #
N-terminal Sequence
Gln23 predicted: no results obtained, sequencing might be blocked
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
122 kDa (monomer)
125-135 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Neuropilin-2

Neuropilin‑2 (Nrp2) is a transmembrane glycoprotein that plays an important role in neuronal axon guidance and development of the vascular system (1). Neuropilin‑2 is differentially expressed in the developing nervous system (2). It binds to Semaphorins 3B, 3C, and 3F, leading to neuronal growth cone collapse (2‑4). This action is important for repulsive axon guidance and accurate axon projection to target fields (4‑7). Neuropilin-2 interacts with a range of proteins that regulate cell growth and morphology. It associates with TGF-beta RI and enhances the ability of TGF‑beta to induce epithelial mesenchymal transition during tumorigenesis (8). It associates with Integrin  alpha 6 beta 1 and promotes alpha 6 beta 1 mediated adhesion to Laminin (9). Neuropilin‑2 additionally binds the heparin‑binding PlGF‑2, HGF, VEGF145, and VEGF165 (10, 11) and associates with VEGF R1, VEGF R2, and VEGF R3 (12, 13). The presence of Neuropilin‑2 on vascular endothelial cells potentiates the angiogenic signaling effects of HGF and VEGF165 (11). Semaphorin 3F, however, can block the contribution of Neuropilin‑2 to angiogenesis (13). In the vascular system, Neuropilin-2 is predominantly expressed on lymphatic vessel and capillary endothelial cells where it cooperates with VEGF R3 to induce lymphatic sprouting (14, 15). Neuropilin‑2 is lost from sympathetic nerve fibers in rheumatoid arthritis (RA) synovium, while a soluble form is elevated in RA synovial fluid (16). Neuropilin‑2 is expressed as an approximately 120 kDa molecule that associates into homo‑oligomers or hetero‑oligomers with Neuropilin‑1 (3, 4). It can be polysialylated during dendritic cell maturation to reach sizes as large as 200 kDa (17). Mature mouse Neuropilin‑2 consists of an 844 amino acid (aa) extracellular domain (ECD) with two CUB domains, two complement factor 5/8‑like domains, one MAM domain, and a Ser-Thr rich region, followed by a 25 aa transmembrane segment and a 42 aa cytoplasmic domain (2). Within the ECD, mouse Neuropilin‑2 shares 94% and 97% aa sequence identity with human and rat Neuropilin‑2, respectively. Alternative splicing of mouse Neuropilin‑2 generates additional isoforms with short deletions in the Ser‑Thr rich region or substitutions of the Ser‑Thr rich region, transmembrane segment, and cytoplasmic domain (2, 18).

  1. Parker, M.W. et al. (2012) Biochemistry 51:9437.
  2. Chen, H. et al. (1997) Neuron 19:547.
  3. Takahashi, T. et al. (1998) Nat. Neurosci. 1:487.
  4. Giger, R.J. et al. (1998) Neuron 21:1079.
  5. Giger, R.J. et al. (2000) Neuron 25:29.
  6. Chen, H. et al. (2000) Neuron 25:43.
  7. Claudepierre, T. et al. (2008) Dev. Dyn. 237:3394.
  8. Grandclement, C. et al. (2011) PLoS ONE 6:e20444.
  9. Goel, H.L. et al. (2012) J. Cell Sci. 125:497.
  10. Gluzman-Poltorak, Z. et al. (2000) J. Biol. Chem. 275:18040.
  11. Sulpice, E. et al. (2008) Blood 111:2036.
  12. Gluzman-Poltorak, Z. et al. (2001) J. Biol. Chem. 276:18688.
  13. Favier, B. et al. (2006) Blood 108:1243.
  14. Yuan, L. et al. (2002) Development 129:4797.
  15. Xu, Y. et al. (2010) J. Cell Biol. 188:115.
  16. Fassold, A. et al. (2009) Arthritis Rheum. 60:2892.
  17. Curreli, S. et al. (2007) J. Biol. Chem. 282:30346.
  18. Rossignol, M. et al. (2000) Genomics 70:211.
Entrez Gene IDs
8828 (Human); 18187 (Mouse); 81527 (Rat)
Alternate Names
MGC126574; neuropilin 2; Neuropilin2; Neuropilin-2; neuropilin-2a(22); neuropilin-2b(0); NP2; NPN 2; NPN2; PRO2714; receptor for VEGF165 and semaphorins class3; Vascular endothelial cell growth factor 165 receptor 2; vascular endothelial growth factor-165 receptor 2; VEGF1265R2; VEGF165R2neuropilin-2a(17)

Citation for Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Alveolar macrophage-derived NRP2 curtails lung injury while boosting host defense in bacterial pneumonia
    Authors: B Wang, W Guo, C Qiu, Y Sun, C Zhao, C Wu, X Lai, X Feng
    Journal of leukocyte biology, 2022;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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