Recombinant Rat Neuropilin-1 Fc Chimera Protein, CF

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566-N1-025
R&D Systems Recombinant Proteins and Enzymes
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Citations (6)
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Recombinant Rat Neuropilin-1 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.1 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized rrNeuropilin-1/Fc Chimera can bind rhVEGF165 with an apparent KD < 1 nM.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived rat Neuropilin-1 protein
Rat Neuropilin-1
Phe22 - Asp854 (Lys811Arg and Pro812 - Gly828 del)
Accession # Q9QWJ9
IEGRDMD Human IgG1
(Pro100 - Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Phe22
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
119 kDa (monomer)
SDS-PAGE
130-150 kDa, reducing conditions

Product Datasheets

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566-N1

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.

566-N1

Formulation Lyophilized from a 0.2 μm filtered solution in Citrate Phosphate and NaCl.
Reconstitution Reconstitute at 200 μg/mL in sterile 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-1

Neuropilin-1 (Npn-1, previously neuropilin; also CD304) is a 130 - 140 kDa type I transmembrane (TM) glycoprotein that regulates axon guidance and angiogenesis (1 - 4). The mature 901 amino acid (aa) rat Npn-1 contains a 623 aa extracellular domain (ECD) that shares 98% aa identity with mouse and 93% aa identity with human, equine, bovine and canine Npn-1 (3, 4). The ECD contains two N-terminal CUB domains, two F5/8 type C domains with homology to coagulation factors V and VIII and a MAM (meprin) domain. In mouse and human, splice variants that lack the TM domain have been described and are either proven or presumed to be soluble antagonists (1, 5 - 7). The sema domains of Class III secreted semaphorins such as Sema3A bind Npn-1 CUB domains (8). The heparin-binding forms of VEGF (VEGF165, VEGF-B and VEGF-E), PlGF (PlGF2), and the C-terminus of Sema3 bind the F5/8 type C domains (8, 9). Npn-1 and Npn-2 share 48% aa identity within the ECD and can form homo- and hetero-oligomers via interaction of their MAM domains (1). Neuropilins show partially overlapping expression in neuronal and endothelial cells during development (1, 2). Both neuropilins act as co-receptors with plexins, mainly plexin A3 and A4, to bind class III semaphorins that mediate axon repulsion (10). However, only Npn-1 binds Sema3A, and only Npn-2 binds Sema3F (1). Both are co-receptors with VEGF R2 (also called KDR or Flk-1) for VEGF165 binding (1). Sema3A signaling can be blocked by VEGF165, which has higher affinity for Npn-1 (11). Npn-1 is preferentially expressed in developing or remodeling arteries (1, 2). Npn-1 is also expressed on dendritic cells and mediates DC-induced T cell proliferation (12).

References
  1. Bielenberg, D.R. et al. (2006) Exp. Cell Res. 312:584. 
  2. Gu, C. et al. (2003) Dev. Cell 5:45. 
  3. He, Z. and M. Tessier-Lavigne (1997) Cell 90:739.
  4. Soker, S. et al. (1998) Cell 92:735.
  5. Gagnon, M.L. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2573. 
  6. Cackowski, F.C. et al. (2004) Genomics 84:82. 
  7. Rossignol, M. et al. (2000) Genomics 70:211.
  8. Gu, C. et al. (2002) J. Biol. Chem. 277:18069.
  9. Mamluk, R. et al. (2002) J. Biol. Chem. 277:24818.
  10. Yaron, A. et al. (2005) Neuron 45:513.
  11. Narazaki, M. and G. Tosato (2006) Blood 107:3892.
  12. Tordjman, R. et al. (2002) Nat. Immunol. 3477.
Entrez Gene IDs
8829 (Human); 18186 (Mouse); 246331 (Rat); 100286859 (Porcine)
Alternate Names
BDCA4; BDCA-4; CD304 antigen; CD304; DKFZp686A03134; DKFZp781F1414; neuropilin 1; Neuropilin1; Neuropilin-1; NP1; NRP; NRP1; transmembrane receptor; Vascular endothelial cell growth factor 165 receptor; VEGF165R

Product Specific Notices

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.

Citations for Recombinant Rat Neuropilin-1 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.

6 Citations: Showing 1 - 6
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  1. Structure-activity relationship study of tetrapeptide inhibitors of the Vascular Endothelial Growth Factor A binding to Neuropilin-1
    Authors: D Tymecka, PFJ Lipi?ski, B Fedorczyk, A Puszko, B Wile?ska, GY Perret, A Misicka
    Peptides, 2017-06-13;0(0):.
    Species: Rat
    Sample Types: Protein
    Applications: ELISA (Capture)
  2. Synergistic Binding of Vascular Endothelial Growth Factor-A and Its Receptors to Heparin Selectively Modulates Complex Affinity.
    Authors: Teran M, Nugent M
    J Biol Chem, 2015-05-15;290(26):16451-62.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  3. The propeptides of VEGF-D determine heparin binding, receptor heterodimerization, and effects on tumor biology.
    Authors: Harris, Nicole C, Davydova, Natalia, Roufail, Sally, Paquet-Fifield, Sophie, Paavonen, Karri, Karnezis, Tara, Zhang, You-Fang, Sato, Teruhiko, Rothacker, Julie, Nice, Edouard, Stacker, Steven A, Achen, Marc G
    J Biol Chem, 2013-02-12;288(12):8176-86.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Precipitation
  4. Low molecular weight fucoidan increases VEGF165-induced endothelial cell migration by enhancing VEGF165 binding to VEGFR-2 and NRP1.
    Authors: Lake AC, Vassy R, Di Benedetto M, Lavigne D, Le Visage C, Perret GY, Letourneur D
    J. Biol. Chem., 2006-10-06;281(49):37844-52.
    Species: Human
    Sample Types: Buffer
    Applications: Bioassay
  5. Localization of heparin- and neuropilin-1-recognition sites of viral VEGFs.
    Authors: Tokunaga Y, Yamazaki Y, Morita T
    Biochem. Biophys. Res. Commun., 2006-07-28;348(3):957-62.
    Species: Virus
    Sample Types: Recombinant Protein
    Applications: Binding Assay
  6. Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A.
    Authors: Narazaki M, Tosato G
    Blood, 2006-01-19;107(10):3892-901.
    Applications: ELISA (Standard)

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Recombinant Rat Neuropilin-1 Fc Chimera Protein, CF
By Rahul Mallick on 08/17/2020
Application: Binding assay/Protein-protein interaction