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

Newer Version Available: 7756-FL
A New rm VEGF R1 is Available! Enhanced purity; ~1.5x better activity; mouse Fc tag; No His-tag!
Catalog # Availability Size / Price Qty
471-F1-100
Product Details
Citations (21)
FAQs
Supplemental Products
Reviews

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

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.
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.
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
Analysis
Ser27
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
110 kDa (monomer)
SDS-PAGE
150-170 kDa, reducing conditions

Product Datasheets

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.

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.
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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

=
÷

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
Entrez Gene IDs
2321 (Human); 14254 (Mouse)
Alternate Names
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

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.

21 Citations: Showing 1 - 10
Filter your results:

Filter by:

  1. Inhibition of FLT1 ameliorates muscular dystrophy phenotype by increased vasculature in a mouse model of Duchenne muscular dystrophy
    Authors: M Verma, Y Shimizu-Mo, Y Asakura, JP Ennen, J Bosco, Z Zhou, GH Fong, S Josiah, D Keefe, A Asakura
    PLoS Genet., 2019;15(12):e1008468.
    Species: Mouse
    Sample Types:
  2. Endophilin-A2 dependent VEGFR2 endocytosis promotes sprouting angiogenesis
    Authors: 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
    Nat Commun, 2019;10(1):2350.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Cell Culture
  3. Blockade of placental growth factor reduces vaso-occlusive complications in murine models of sickle cell disease
    Authors: JM Gu, S Yuan, D Sim, K Abe, P Liu, M Rosenbruch, P Bringmann, K Kauser
    Exp. Hematol., 2018;0(0):.
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Binding Assay
  4. Extracellular Protein Fibulin-7 and Its C-Terminal Fragment Have In Vivo Antiangiogenic Activity
    Authors: T Ikeuchi, S de Vega, P Forcinito, AD Doyle, J Amaral, IR Rodriguez, E Arikawa-Hi, Y Yamada
    Sci Rep, 2018;8(1):17654.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. A paradoxical method to enhance compensatory lung growth: Utilizing a VEGF inhibitor
    Authors: 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
    PLoS ONE, 2018;13(12):e0208579.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  6. Role of retinal pigment epithelium-derived exosomes and autophagy in new blood vessel formation
    Authors: 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
    J. Cell. Mol. Med., 2018;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Hyperoxia causes regression of vitreous neovascularization by downregulating VEGF/VEGFR2 pathway.
    Authors: Liu, Hua, Zhang, Wenbo, Xu, Zhimin, Caldwell, Robert W, Caldwell, Ruth B, Brooks, Steven E
    Invest Ophthalmol Vis Sci, 2013;54(2):918-31.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  8. Angiopoietins/TIE2 system and VEGF are involved in ovarian function in a DHEA rat model of polycystic ovary syndrome.
    Authors: Abramovich D, Irusta G, Bas D, Cataldi NI, Parborell F, Tesone M
    Endocrinology, 2012;153(7):3446-56.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  9. Role of reactive oxygen species during hypertension in response to chronic antiangiogenic factor (sFlt-1) excess in pregnant rats.
    Authors: Tam Tam KB, Lamarca B, Arany M, Cockrell K, Fournier L, Murphy S, Martin JN, Granger JP
    Am. J. Hypertens., 2011;24(1):110-3.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  10. Sema3E-PlexinD1 signaling selectively suppresses disoriented angiogenesis in ischemic retinopathy in mice.
    Authors: Fukushima Y, Okada M, Kataoka H
    J. Clin. Invest., 2011;121(5):1974-85.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  11. Administrations of peripheral blood CD34-positive cells contribute to medial collateral ligament healing via vasculogenesis.
    Authors: Tei K, Matsumoto T, Mifune Y, Ishida K, Sasaki K, Shoji T, Kubo S, Kawamoto A, Asahara T, Kurosaka M, Kuroda R
    Stem Cells, 2008;26(3):819-30.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  12. Leukemia inhibitory factor regulates microvessel density by modulating oxygen-dependent VEGF expression in mice.
    Authors: Kubota Y, Hirashima M, Kishi K, Stewart CL, Suda T
    J. Clin. Invest., 2008;118(7):2393-403.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  13. Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1.
    Authors: Ponticelli S, Marasco D, Tarallo V, Albuquerque RJ, Mitola S, Takeda A, Stassen JM, Presta M, Ambati J, Ruvo M, De Falco S
    J. Biol. Chem., 2008;283(49):34250-9.
    Species: Synthetic
    Sample Types: Protein
    Applications: Binding Assay
  14. Soluble vascular endothelial growth factor receptor-1 protects mice in sepsis.
    Authors: Tsao PN, Chan FT, Wei SC, Hsieh WS, Chou HC, Su YN, Chen CY, Hsu WM, Hsieh FJ, Hsu SM
    Crit. Care Med., 2007;35(8):1955-60.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  15. Corneal avascularity is due to soluble VEGF receptor-1.
    Authors: Ambati BK, Nozaki M, Singh N, Takeda A, Jani PD, Suthar T, Albuquerque RJ, Richter E, Sakurai E, Newcomb MT, Kleinman ME, Caldwell RB, Lin Q, Ogura Y, Orecchia A, Samuelson DA, Agnew DW, St Leger J, Green WR, Mahasreshti PJ, Curiel DT, Kwan D, Marsh H, Ikeda S, Leiper LJ, Collinson JM, Bogdanovich S, Khurana TS, Shibuya M, Baldwin ME, Ferrara N, Gerber HP, De Falco S, Witta J, Baffi JZ, Raisler BJ, Ambati J
    Nature, 2006;443(7114):993-7.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  16. Therapeutic potential of vasculogenesis and osteogenesis promoted by peripheral blood CD34-positive cells for functional bone healing.
    Authors: Matsumoto T, Kawamoto A, Kuroda R, Ishikawa M, Mifune Y, Iwasaki H, Miwa M, Horii M, Hayashi S, Oyamada A, Nishimura H, Murasawa S, Doita M, Kurosaka M, Asahara T
    Am. J. Pathol., 2006;169(4):1440-57.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  17. Placenta growth factor in diabetic wound healing: altered expression and therapeutic potential.
    Authors: Cianfarani F, Zambruno G, Brogelli L, Sera F, Lacal PM, Pesce M, Capogrossi MC, Failla CM, Napolitano M, Odorisio T
    Am. J. Pathol., 2006;169(4):1167-82.
    Species: N/A
    Sample Types: N/A
    Applications: ELISA (Standard)
  18. Antagonism of vascular endothelial growth factor results in microvessel attrition and disorganization of wound tissue.
    Authors: Gudehithlu KP, Ahmed N, Wu H, Litbarg NO, Garber SL, Arruda JA, Dunea G, Singh AK
    J. Lab. Clin. Med., 2005;145(4):194-203.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  19. VEGF receptor 1 signaling is essential for osteoclast development and bone marrow formation in colony-stimulating factor 1-deficient mice.
    Authors: Niida S, Kondo T, Hiratsuka S, Hayashi S, Amizuka N, Noda T, Ikeda K, Shibuya M
    Proc. Natl. Acad. Sci. U.S.A., 2005;102(39):14016-21.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  20. Neutralization of circulating vascular endothelial growth factor (VEGF) by anti-VEGF antibodies and soluble VEGF receptor 1 (sFlt-1) induces proteinuria.
    Authors: Sugimoto H, Hamano Y, Charytan D, Cosgrove D, Kieran M, Sudhakar A, Kalluri R
    J. Biol. Chem., 2003;278(15):12605-8.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  21. VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia.
    Authors: Gerhardt H, Golding M, Fruttiger M, Ruhrberg C, Lundkvist A, Abramsson A, Jeltsch M, Mitchell C, Alitalo K, Shima D, Betsholtz C
    J. Cell Biol., 2003;161(6):1163-77.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo

FAQs

No product specific FAQs exist for this product, however you may

View all Proteins and Enzyme FAQs

Reconstitution Buffers

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

There are currently no reviews for this product. Be the first to review Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF and earn rewards!

Have you used Recombinant Mouse VEGFR1/Flt-1 Fc Chimera Protein, CF?

Submit a review and receive an Amazon gift card.

$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image

$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image

Submit a Review