Recombinant Human Neuropilin-1 Fc Chimera Protein, CF
Recombinant Human Neuropilin-1 Fc Chimera Protein, CF Summary
Product Specifications
Human Neuropilin-1 (Phe22-Lys852) Accession # NP_003864.4 | IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
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.
10455-N1
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
When Recombinant Human Neuropilin-1 Fc Chimera (Catalog # 10445-N1) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human VEGF 165 (Catalog # 293-VE) binds with an ED50 of 0.25-1.5 ng/mL.
2 µg/lane of Recombinant Human Neuropilin-1 Fc Chimera (Catalog # 10455-N1) was resolved by SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 117-131 kDa and 220-250 kDa, respectively.
Reconstitution Calculator
Background: Neuropilin-1
Neuropilin-1 (Npn-1, also known as neuropilin and CD304) is a 130-140 kDa type I transmembrane (TM) glycoprotein that regulates axon guidance and angiogenesis (1-4). The full-length 923 amino acid (aa) human Npn-1 isoform 1 contains an 835 aa extracellular domain (ECD) that shows 92-95% aa identity with mouse, rat, bovine and canine Npn-1 (3, 4). The ECD contains two N-terminal CUB domains (termed a1a2), two domains with homology to coagulation factors V and VIII (b1b2) and a MAM (meprin) domain (c). C-terminally divergent splice variants with 704, 644, 609, and 551 aa lack the MAM and TM domains and are demonstrated or presumed to be soluble antagonists (1, 5-7). A 906 aa form lacks a TM segment, but secretion has not been found (8). The sema domains of Class III secreted semaphorins such as Sema3A bind Npn-1 a1a2 (9). Heparin, the heparin-binding forms of VEGF (VEGF 165, VEGF-B and VEGF-E), PlGF (PlGF2), and the C-terminus of Sema3 bind the b1b2 region (9, 10). 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 (11). 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 VEGF 165 binding (1). Sema3A signaling can be blocked by VEGF 165, which has higher affinity for Npn-1 (12). Npn-1 is preferentially expressed in arteries during development or those undergoing remodeling (1, 2). Npn-1 is also expressed on dendritic cells and mediates DC-induced T cell proliferation (13). Npn-1 is a marker of CD4+ Treg cells and a population of CD8+ T-cells infiltrating solid tumors. Immunotherapies that block Npn-1 synergizes with anti-PD-1 to enhance CD8+ proliferation and response (14). There is evidence that Npn-1 with VEGF-A plays a role in stemness of breast cancer cell by activating Wnt/b-catenin pathway (15).
- Bielenberg, D.R. et al. (2006) Exp. Cell Res. 312:584.
- Gu, C. et al. (2003) Dev. Cell 5:45.
- He, Z. and M. Tessier-Lavigne (1997) Cell 90:739.
- Soker, S. et al. (1998) Cell 92:735.
- Gagnon, M.L. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2573.
- Cackowski, F.C. et al. (2004) Genomics 84:82.
- Rossignol, M. et al. (2000) Genomics 70:211.
- Tao, Q. et al. (2003) Angiogenesis 6:39.
- Gu, C. et al. (2002) J. Biol. Chem. 277:18069.
- Mamluk, R. et al. (2002) J. Biol. Chem. 277:24818.
- Yaron, A. et al. (2005) Neuron 45:513.
- Narazaki, M. and G. Tosato (2006) Blood 107:3892.
- Tordjman, R. et al. (2002) Nat. Immunol. 3:477.
- Leclerc, M. et al. (2019) Nat Commun. 10:3345.
- Zhang, L. et al. (2017) Cell Physiol. Biochem. 44:1251.
Citations for Recombinant Human 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.
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Neuropilin 1 and its inhibitory ligand mini-tryptophanyl-tRNA synthetase inversely regulate VE-cadherin turnover and vascular permeability
Authors: N Gioelli, LJ Neilson, N Wei, G Villari, W Chen, B Kuhle, M Ehling, F Maione, S Willox, S Brundu, D Avanzato, G Koulouras, M Mazzone, E Giraudo, XL Yang, D Valdembri, S Zanivan, G Serini
Nature Communications, 2022-07-20;13(1):4188.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay -
Overexpressed Neuropilin-1 in Endothelial Cells Promotes Endothelial Permeability through Interaction with ANGPTL4 and VEGF in Kawasaki Disease
Authors: J Huang, S Zhang
Mediators of Inflammation, 2021-08-13;2021(0):9914071.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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