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Recombinant Human Neuropilin-2 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human Neuropilin-2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human (rh) Neuropilin‑2 Fc Chimera can bind rhVEGF165 with an apparent KD < 5 nM.
Source
Mouse myeloma cell line, NS0-derived human Neuropilin-2 protein
Human Neuropilin-2
(Gln23-Tyr855)
Accession #Q7LBX6
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln23 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
NRP2
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
120.5 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
140 kDa, reducing conditions
Publications
Read Publications using
2215-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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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.

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

Alternate Names for Recombinant Human 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 (Npn-2) is a 120 kDa, type I transmembrane (TM) glycoprotein that is related to the semaphorin receptor now known as Neuropilin-1 (1). Npn-2 is a complex molecule with multiple splice forms. Five transmembrane forms are known, and one 62 kDa soluble form has been identified (2). Based on the originally reported precursor size of 909 amino acids (aa), the “standard” precursor in human will have a 20 aa signal sequence, an 842 aa extracellular region, a 25 aa TM segment, and a 42 aa cytoplasmic tail (1). The extracellular region contains two N-terminal CUB (C1r/Ugef/BMP-1) domains, two jellyroll-shaped coagulation factor V type C domains, and a juxtamembrane MAM (meprin/A-5 protein/tyrosine phosphatase μ) domain (1, 3). The CUB and factor V domain are involved in VEGF and semaphorin binding. The MAM domain appears necessary for signaling through plexin-1 (4). The five transmembrane isoforms all share the same CUB, factor V and MAM domains. Splicing begins at aa 809, seven amino acids after the end of the MAM domain, and it involves the end of the extracellular region, the TM segment, and the cytoplasmic domain (a total of 101 aa). Two of the four variants show a complete replacement of these 101 aa with a totally unrelated stretch of approximately 90 aa. This creates a new TM and cytoplasmic tail. These forms are called “Npn-2b” forms. Two other isoforms (plus the standard 909 aa form) retain the 101 aa stretch, and add either 17 or 22 aa to the end of the extracellular region. These forms are called “Npn-2a” forms. The isoform offered by R&D Systems is the “a” form with the 17 aa addition. This isoform shows 94% aa identity to the equivalent regions in mouse and rat Npn-2. The soluble form of Npn-2 is 555 aa in precursor length, and contains the two CUB domains plus the first 1½ factor V type C domains (1). Npn-2 binds Sema3B through F, and VEGF isoforms 165, 145, PlGF-2 and VEGF-C (5). It is known to form homodimers and heterodimers with Npn-1, and it forms receptor complexes with plexin-1 and VEGF R1 (4, 5). Npn-2 is found on a variety of cell types including neurons (motor, autonomic, sensory), vascular endothelial cells, Schwann cells and pancreatic acinar cells.

  1. Chen, H. et al. (1997) Neuron 19:547.
  2. Rossignol, M. et al. (2000) Genomics 70:211.
  3. He, Z. and M. Tessier-lavigne (1997) Cell 90:739.
  4. Nakamura, F. and Y. Goshima (2002) Adv. Exp. Med. Biol. 515:55.
  5. Neufeld, G. et al. (2002) Adv. Exp. Med. Biol. 515:81.

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Publications for Neuropilin-2 (2215-N2)(9)

We have publications tested in 3 confirmed species: Human, Mouse, Virus.

We have publications tested in 6 applications: Binding Assay, Bioassay, Biolayer Interferometry (BLI), ELISA (Standard), Surface Plasmon Resonance, Surface Plasmon Resonance (SPR.


Filter By Application
Binding Assay
(1)
Bioassay
(6)
Biolayer Interferometry (BLI)
(1)
ELISA (Standard)
(1)
Surface Plasmon Resonance
(1)
Surface Plasmon Resonance (SPR
(1)
All Applications
Filter By Species
Human
(6)
Mouse
(1)
Virus
(1)
All Species
Showing Publications 1 - 9 of 9.
Publications using 2215-N2 Applications Species
C Fornara, E Schultz, D Lilleri, F Baldanti, B Ryckman, G Gerna Fibroblast, Epithelial and Endothelial Cell-Derived Human Cytomegalovirus Strains Display Distinct Neutralizing Antibody Responses and Varying Levels of gH/gL Complexes International Journal of Molecular Sciences, 2023-02-23;24(5):. 2023-02-23 [PMID: 36901847] (Bioassay, Human) Bioassay Human
B Braun, K Laib Sampa, AK Kuderna, M Widmann, C Sinzger Viral and Cellular Factors Contributing to the Hematogenous Dissemination of Human Cytomegalovirus via Polymorphonuclear Leukocytes Viruses, 2022-07-18;14(7):. 2022-07-18 [PMID: 35891541] (Bioassay, Human) Bioassay Human
S Dutta, NS Polavaram, R Islam, S Bhattachar, S Bodas, T Mayr, S Roy, SAY Albala, MI Toma, A Darehshour, A Borkowetz, S Conrad, S Fuessel, M Wirth, GB Baretton, LC Hofbauer, P Ghosh, KJ Pienta, DL Klinkebiel, SK Batra, MH Muders, K Datta Neuropilin-2 regulates androgen-receptor transcriptional activity in advanced prostate cancer Oncogene, 2022-06-27;0(0):. 2022-06-27 [PMID: 35754042] (Bioassay, Human) Bioassay Human
Martinez-Martin N, Marcandalli J, Huang C, Arthur C, Perotti M, Foglierini M, Ho H, Dosey A, Shriver S, Payandeh J, Leitner A, Lanzavecchia A, Perez L, Ciferri C An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a Central Viral Receptor. Cell, 2018-07-26;174(5):1158-1171.e19. 2018-07-26 [PMID: 30057110] (Biolayer Interferometry (BLI), Surface Plasmon Resonance (SPR, Virus) Biolayer Interferometry (BLI), Surface Plasmon Resonance (SPR Virus
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 The propeptides of VEGF-D determine heparin binding, receptor heterodimerization, and effects on tumor biology. J Biol Chem, 2013-02-12;288(12):8176-86. 2013-02-12 [PMID: 23404505] (Bioassay, Human) Bioassay Human
Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Narazaki M, Segarra M, Hou X, Tanaka T, Li X, Tosato G Oligo-guanosine nucleotide induces neuropilin-1 internalization in endothelial cells and inhibits angiogenesis. Blood, 2010-07-06;116(16):3099-107. 2010-07-06 [PMID: 20606164] (Binding Assay, Surface Plasmon Resonance, Human) Binding Assay, Surface Plasmon Resonance Human
Fassold A, Falk W, Anders S, Hirsch T, Mirsky VM, Straub RH Soluble neuropilin-2, a nerve repellent receptor, is increased in rheumatoid arthritis synovium and aggravates sympathetic fiber repulsion and arthritis. Arthritis Rheum., 2009-10-01;60(10):2892-901. 2009-10-01 [PMID: 19790074] (ELISA (Standard)) ELISA (Standard)
Jaalouk DE, Ozawa MG, Sun J, Lahdenranta J, Schlingemann RO, Pasqualini R, Arap W The original Pathologische Anatomie Leiden-Endothelium monoclonal antibody recognizes a vascular endothelial growth factor binding site within neuropilin-1. Cancer Res., 2007-10-15;67(20):9623-9. 2007-10-15 [PMID: 17942890] (Bioassay, Mouse) Bioassay Mouse

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Bioinformatics

Gene Symbol NRP2
Uniprot