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

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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 C-terminus
Accession #
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
  • Bioactivity
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:

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.
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

  • EC 2.7.10
  • EC 2.7.10.1
  • 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

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).
  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.

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Publications for VEGFR1/Flt-1 (471-F1)(26)

We have publications tested in 3 confirmed species: Human, Mouse, Rat.

We have publications tested in 7 applications: Binding Assay, Bioassay, Cell Culture, ELISA (Standard), Functional Assay, In Vivo, Surface Plasmon Resonance.


Filter By Application
Binding Assay
(2)
Bioassay
(6)
Cell Culture
(1)
ELISA (Standard)
(1)
Functional Assay
(1)
In Vivo
(14)
Surface Plasmon Resonance
(1)
All Applications
Filter By Species
Human
(2)
Mouse
(18)
Rat
(5)
All Species
Showing Publications 1 - 10 of 26. Show All 26 Publications.
Publications using 471-F1 Applications Species
X Huang, L Jia, Y Jia, X Xu, R Wang, M Wei, H Li, H Peng, Y Wei, Q He, K Wang sFlt-1-enriched exosomes induced endothelial cell dysfunction and a preeclampsia-like phenotype in mice Cytokine, 2023-04-14;166(0):156190. 2023-04-14 [PMID: 37062152] (Bioassay, Mouse) Bioassay Mouse
N Popovic, E Hooker, A Barabino, A Flamier, F Provost, M Buscarlet, G Bernier, B Larrivée COCO/DAND5 inhibits developmental and pathological ocular angiogenesis Embo Molecular Medicine, 2021-02-15;0(0):e12005. 2021-02-15 [PMID: 33587337] (Bioassay, Mouse) Bioassay Mouse
B Di Marco, EE Crouch, B Shah, C Duman, MF Paredes, C Ruiz de Al, EJ Huang, J Alfonso Reciprocal Interaction between Vascular Filopodia and Neural Stem Cells Shapes Neurogenesis in the Ventral Telencephalon Cell Rep, 2020-10-13;33(2):108256. 2020-10-13 [PMID: 33053356] (Bioassay, Mouse) Bioassay Mouse
V Mashayekhi, KT Xenaki, PMP van Bergen, S Oliveira Dual Targeting of Endothelial and Cancer Cells Potentiates In Vitro Nanobody-Targeted Photodynamic Therapy Cancers, 2020-09-23;12(10):. 2020-09-23 [PMID: 32977602] (Functional Assay, Mouse) Functional Assay Mouse
M Verma, Y Shimizu-Mo, Y Asakura, JP Ennen, J Bosco, Z Zhou, GH Fong, S Josiah, D Keefe, A Asakura Inhibition of FLT1 ameliorates muscular dystrophy phenotype by increased vasculature in a mouse model of Duchenne muscular dystrophy PLoS Genet., 2019-12-26;15(12):e1008468. 2019-12-26 [PMID: 31877123] (Surface Plasmon Resonance, Mouse) Surface Plasmon Resonance Mouse
G Genet, K Boyé, T Mathivet, R Ola, F Zhang, A Dubrac, J Li, N Genet, L Henrique G, L Benedetti, S Künzel, L Pibouin-Fr, JL Thomas, A Eichmann Endophilin-A2 dependent VEGFR2 endocytosis promotes sprouting angiogenesis Nat Commun, 2019-05-28;10(1):2350. 2019-05-28 [PMID: 31138815] (Cell Culture, Mouse) Cell Culture Mouse
DT Dao, L Anez-Busti, SS Jabbouri, A Pan, H Kishikawa, PD Mitchell, GL Fell, MA Baker, RS Watnick, H Chen, MS Rogers, DR Bielenberg, M Puder A paradoxical method to enhance compensatory lung growth: Utilizing a VEGF inhibitor PLoS ONE, 2018-12-19;13(12):e0208579. 2018-12-19 [PMID: 30566445] (In Vivo, Mouse) In Vivo Mouse
T Ikeuchi, S de Vega, P Forcinito, AD Doyle, J Amaral, IR Rodriguez, E Arikawa-Hi, Y Yamada Extracellular Protein Fibulin-7 and Its C-Terminal Fragment Have In Vivo Antiangiogenic Activity Sci Rep, 2018-12-05;8(1):17654. 2018-12-05 [PMID: 30518776] (Bioassay, Human) Bioassay Human
S Atienzar-A, G Serrano-He, A Freire Val, C Ruiz de Al, M Muriach, JM Barcia, JM Garcia-Ver, FJ Romero, J Sancho-Pel Role of retinal pigment epithelium-derived exosomes and autophagy in new blood vessel formation J. Cell. Mol. Med., 2018-08-21;0(0):. 2018-08-21 [PMID: 30133118] (Bioassay, Human) Bioassay Human
JM Gu, S Yuan, D Sim, K Abe, P Liu, M Rosenbruch, P Bringmann, K Kauser Blockade of placental growth factor reduces vaso-occlusive complications in murine models of sickle cell disease Exp. Hematol., 2018-01-11;0(0):. 2018-01-11 [PMID: 29337222] (Binding Assay, Mouse) Binding Assay Mouse
Show All 26 Publications.

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Bioinformatics

Gene Symbol Flt1
Uniprot