Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF Summary
Details of Functionality |
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. |
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 |
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C-terminus |
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Accession # |
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N-terminal Sequence |
Ser27 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Flt1 |
Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
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Theoretical MW |
110 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 |
150-170 kDa, reducing conditions |
Publications |
Read Publications using 471-F1 in the following applications:
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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.
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Buffer |
Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CHAPS. |
Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF
Background
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).
- Otrock, Z.K. et al. (2007) Blood Cells Mol. Dis. 38:258.
- Peters, K.G. et al. (1993) Proc. Natl. Acad. Sci. USA 90:8915.
- Murakami, M. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:658.
- Al-Ani, B. et al. (2010) Hypertension 55:689.
- Rahimi, N. et al. (2009) Cancer Res. 69:2607.
- He, Y. et al. (1999) Molecular Endocrinology 13:537.
- Cai, J. et al. (2012) EMBO Mol. Med. 4:980.
- Kendall, R.L. and K.A. Thomas (1993) Proc. Natl. Acad. Sci. USA 90:10705.
- Sawano, A. et al. (1996) Cell Growth Differ. 7:213.
- Barleon, B. et al. (1997) J. Biol. Chem. 272:10382.
- Kappas, N.C. et al. (2008) J. Cell Biol. 181:847.
- Mac Gabhann, F. and A.S. Popel (2007) Biophys. Chem. 128:125.
- Hiratsuka, S. et al. (1998) Proc. Natl. Acad. Sci. USA 95:9349.
- Fong, G.H. et al. (1995) Nature 376:66.
- Nishi, J. et al. (2008) Circ. Res. 103:261.
- Muramatsu, M. et al. (2010) Cancer Res. 70:8211.
- Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
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