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Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF Summary

Details of Functionality
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.
Source
Mouse myeloma cell line, NS0-derived mouse Neuropilin-2 protein
Mouse Neuropilin-2
(Gln23-Asp863)
Accession # O35375
IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Gln23 predicted: no results obtained, sequencing might be blocked
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Nrp2
Purity
>95%, by SDS-PAGE with silver staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
122 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
125-135 kDa, reducing conditions
Publications
Read Publication using
7988-N2 in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

  • 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)

Background

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.

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Publications for Neuropilin-2 (7988-N2)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol Nrp2
Uniprot