Recombinant Rat Neuropilin-2 Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 567-N2

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

Source

NS0

Accession #

O35276

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Binding Activity

View all Neuropilin-2 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived rat Neuropilin-2 protein
Rat Neuropilin-2
Gln23-Asp857 (Val809-Asp825 del)
Accession # O35276		 IEGRDMD Human IgG1
(Pro100-Lys330)		 6-His tag
N-terminus C-terminus

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

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

N-terminal Sequence Analysis

No results obtained: Gln23 predicted

Predicted Molecular Mass

120 kDa (monomer)

SDS-PAGE

130-150 kDa, reducing conditions

Activity

Measured by its binding ability in a functional ELISA.
Immobilized Recombinant Rat Neuropilin‑2 Fc Chimera at 5 µg/mL (100 µL/well) can bind recombinant human VEGF165 in the presence of 2 µg/mL of heparin with an apparent Kd <1nM.

Formulation, Preparation and Storage

567-N2
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 200 μg/mL in sterile 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 rat Neuropilin-2 consists of an 836 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 (18). Within the ECD, rat Neuropilin-2 shares 93% and 97% aa sequence identity with human and mouse Neuropilin-2, respectively.

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. Kolodkin, A.L. et al. (1997) Cell 90:753.

Alternate Names

Neuropilin2

Entrez Gene IDs

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

Gene Symbol

NRP2

UniProt

O35276

Additional Neuropilin-2 Products

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

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Rat Neuropilin-2 Fc Chimera Protein, CF

This product or the use of this product is covered by U.S. Patents owned by The Regents of the University of California. This product is for research use only and is not to be used for commercial purposes. Use of this product to produce products for sale or for diagnostic, therapeutic or drug discovery purposes is prohibited.

In order to obtain a license to use this product for such purposes, contact The Regents of the University of California.U.S. Patent # 6,054,293, 6,623,738, and other U.S. and international patents pending.

For research use only

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