Recombinant Rat Neuropilin-1 Fc Chimera Protein, CF
Recombinant Rat Neuropilin-1 Fc Chimera Protein, CF Summary
Phe22 - Asp854 (Lys811Arg and Pro812 - Gly828 del)
Accession # Q9QWJ9
(Pro100 - Lys330)
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.
|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.
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).
- 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.
- 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. 3477.
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.
Citations: Showing 1 - 5
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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
Sample Types: Protein
Applications: ELISA (Capture)
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;290(26):16451-62.
Sample Types: Protein
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;281(49):37844-52.
Sample Types: Buffer
Localization of heparin- and neuropilin-1-recognition sites of viral VEGFs.
Authors: Tokunaga Y, Yamazaki Y, Morita T
Biochem. Biophys. Res. Commun., 2006;348(3):957-62.
Sample Types: Recombinant Protein
Applications: Binding Assay
Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A.
Authors: Narazaki M, Tosato G
Sample Types: N/A
Applications: ELISA (Standard)
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