Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7988-N2

R&D Systems, part of Bio-Techne
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7988-N2-025
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Key Product Details

Source

NS0

Accession #

O35375

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all Neuropilin-2 Proteins and Enzymes »

Product Specifications

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

Purity

>95%, by SDS-PAGE with silver staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Gln23 predicted: no results obtained, sequencing might be blocked

Predicted Molecular Mass

122 kDa (monomer)

SDS-PAGE

125-135 kDa, reducing conditions

Activity

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.

Formulation, Preparation and Storage

7988-N2
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

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  alpha6 beta1 and promotes alpha6 beta1 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).

References

  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.

Alternate Names

Neuropilin2

Entrez Gene IDs

8828 (Human); 18187 (Mouse); 81527 (Rat)

Gene Symbol

NRP2

UniProt

O35375

Additional Neuropilin-2 Products

Product Documents for Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

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