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

R&D Systems, part of Bio-Techne | Catalog # 471-F1

R&D Systems, part of Bio-Techne
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471-F1-100
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Key Product Details

Source

NS0

Accession #

P35969

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all VEGFR1/Flt-1 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse VEGFR1/Flt-1 protein
Mouse VEGFR1
(Ser27-Glu759)
Accession # P35969		 IEGRMD Human IgG1
(Pro100-Lys330)		 6-His tag
N-terminus C-terminus

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ser27

Predicted Molecular Mass

110 kDa (monomer)

SDS-PAGE

150-170 kDa, reducing conditions

Activity

Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323.
The ED50 for this effect is 10-30 ng/mL.

Formulation, Preparation and Storage

471-F1
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CHAPS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

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 autophosphorylation 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).

References

  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

Alternate Names

Flt-1, FLT1, FRT, VEGF R1, VEGFR-1

Entrez Gene IDs

2321 (Human); 14254 (Mouse)

Gene Symbol

FLT1

UniProt

P35969

Additional VEGFR1/Flt-1 Products

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

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Product Specific Notices for Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF

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