Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF

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Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 5-30 ng/mL.
Mouse myeloma cell line, NS0-derived mouse VEGFR1/Flt-1 protein
Mouse VEGFR1
Accession # P35969
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
109.6 kDa (monomer)
130-150 kDa, reducing conditions

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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.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in 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: VEGFR1/Flt-1

VEGFR1 (vascular endothelial growth factor receptor 1), also called Flt‑1 (Fms‑like tyrosine kinase), is a 180 kDa type I transmembrane glycoprotein in the class III subfamily of receptor tyrosine kinases (RTKs) (1, 2). While family members VEGFR1, VEGFR2/KDR/Flk‑1 and VEGFR3/Flt‑4 are all mainly expressed on endothelial cells and play central roles in vasculogenesis, angiogenesis, and lymphangiogenesis, only VEGFR1 is expressed on macrophages, and mainly plays inhibitory roles (1‑3). VEGFR1 expression is also reported on osteoblasts, placental trophoblasts, renal mesangial cells, and some hematopoietic stem cells (1, 2). Like other class III RTKs, mouse VEGFR1 contains a signal peptide (aa 1‑22), an extracellular domain (ECD aa 23‑759) with seven Ig‑like repeats, a transmembrane domain (aa 760‑781) and a cytoplasmic region (aa 782‑1333) with a tyrosine kinase domain and several autocatalytic phosphotyrosine sites. Mouse VEGFR1 ECD shares 91% aa sequence identity with rat and 76‑79% with human, equine, canine and porcine VEGFR1. Soluble forms of the VEGFR1 ECD are produced by alternative splicing, and may also be shed during regulated intracellular proteolysis (4‑10). Both soluble and transmembrane forms can inhibit angiogenesis by binding and sequestering its ligands, VEGF (VEGF‑A), VEGF‑B or PlGF (6‑11). VEGFR1 dimerizes upon ligand binding, which can include heterodimerization with VEGFR2 that modifies VEGFR2‑mediated endothelial proliferation and vessel branching (8, 11, 12). VEGFR1 binds VEGF with higher affinity than does VEGFR2, but shows weaker kinase activity (9, 13). Both PlGF and VEGF induce phosphorylation of transmembrane VEGFR1 (5, 9, 13). While deletion of mouse VEGFR1 is lethal due to overgrowth and disorganization of the vasculature, kinase‑inactive mutants are viable (13, 14). VEGFR1 is up‑regulated during hypoxia, and participates in neovascularization and wound healing (1, 2, 15). VEGFR1 engagement on monocyte/macrophage lineage cells enhances their migration, and release of growth factors and cytokines (1, 3, 13, 16). Lymphangiogenesis, angiogenesis, and growth‑promoting effects of VEGFR1 are thought to result from enhanced migration of macrophages from the bone marrow to tumors and tissues where they recruit endothelial progenitors (3, 16). Circulating levels of VEGFR1 increase during pregnancy and are further elevated in preeclampsia (4, 6, 17).

  1. Otrock, Z.K. et al. (2007) Blood Cells Mol. Dis. 38:258.
  2. Peters, K.G. et al. (1993) Proc. Natl. Acad. Sci. USA 90:8915.
  3. Murakami, M. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:658.
  4. Al-Ani, B. et al. (2010) Hypertension 55:689.
  5. Rahimi, N. et al. (2009) Cancer Res. 69:2607.
  6. He, Y. et al. (1999) Molecular Endocrinology 13:537.
  7. Cai, J. et al. (2012) EMBO Mol. Med. 4:980.
  8. Kendall, R.L. and K.A. Thomas (1993) Proc. Natl. Acad. Sci. USA 90:10705.
  9. Sawano, A. et al. (1996) Cell Growth Differ. 7:213.
  10. Barleon, B. et al. (1997) J. Biol. Chem. 272:10382.
  11. Kappas, N.C. et al. (2008) J. Cell Biol. 181:847.
  12. Mac Gabhann, F. and A.S. Popel (2007) Biophys. Chem. 128:125.
  13. Hiratsuka, S. et al. (1998) Proc. Natl. Acad. Sci. USA 95:9349.
  14. Fong, G.H. et al. (1995) Nature 376:66.
  15. Nishi, J. et al. (2008) Circ. Res. 103:261.
  16. Muramatsu, M. et al. (2010) Cancer Res. 70:8211.
  17. Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
Long Name
Vascular Endothelial Growth Factor Receptor 1
Entrez Gene IDs
2321 (Human); 14254 (Mouse)
Alternate Names
EC 2.7.10; EC; FLT; FLT1; Flt-1; Fms-like tyrosine kinase 1; fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascularpermeability factor receptor); FRT; Tyrosine-protein kinase FRT; Tyrosine-protein kinase receptor FLT; vascular endothelial growth factor receptor 1; Vascular permeability factor receptor; VEGF R1; VEGFR1; VEGFR-1

Citations for Recombinant Mouse VEGFR1/Flt-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.

3 Citations: Showing 1 - 3
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  1. A potential regulatory network among WDR86-AS1, miR-10b-3p, and LITAF is possibly involved in preeclampsia pathogenesis
    Authors: R Li, N Wang, M Xue, W Long, C Cheng, C Mi, Z Gao
    Cell. Signal., 2018;0(0):.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  2. A novel in vivo model of puncture-induced iris neovascularization
    Authors: O Beaujean, F Locri, M Aronsson, A Kvanta, H André
    PLoS ONE, 2017;12(6):e0180235.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  3. Photoreceptor avascular privilege is shielded by soluble VEGF receptor-1.
    Authors: Luo, Ling, Uehara, Hironori, Zhang, Xiaohui, Das, Subrata, Olsen, Thomas, Holt, Derick, Simonis, Jacquely, Jackman, Kyle, Singh, Nirbhai, Miya, Tadashi, Huang, Wei, Ahmed, Faisal, Bastos-Carvalho, Ana, Le, Yun Zhen, Mamalis, Christin, Chiodo, Vince A, Hauswirth, William, Baffi, Judit, Lacal, Pedro M, Orecchia, Angela, Ferrara, Napoleon, Gao, Guangpin, Young-Hee, Kim, Fu, Yingbin, Owen, Leah, Albuquerque, Romulo, Baehr, Wolfgang, Thomas, Kirk, Li, Dean Y, Chalam, Kakarla, Shibuya, Masabumi, Grisanti, Salvator, Wilson, David J, Ambati, Jayakris, Ambati, Balamura
    Elife, 2013;2(0):e00324.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo


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