Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, CF
Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, CF Summary
Product Specifications
Human VEGFR1 (Ser27-lle328) Accession #P17948 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
3516-FL
Carrier Free
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.
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.
3516-FL
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
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.
|
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, human VEGFR1 contains a signal peptide (aa 1-22), an extracellular domain (ECD aa 27-758) with seven Ig-like repeats, a transmembrane domain (aa 759-780) and a cytoplasmic region (aa 781-1338) with a tyrosine kinase domain and several autocatalytic phosphotyrosine sites. Human VEGFR1 ECD shares 78%, 78%, 84%, 87%, and 90% aa sequence identity with mouse, rat, porcine, canine and equine VEGFR1, respectively. 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 upregulated during hypoxia, and participates in neovascularization and wound healing (1, 2, 15). VEGF R1 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.
Citation for Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, 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.
1 Citation: Showing 1 - 1
-
Soluble VEGF receptor 1 (sFLT1) induces non-apoptotic death in ovarian and colorectal cancer cells.
Authors: Tatsuya Miyake, Keiichi Kumasawa, Noriko Sato, Tsuyoshi Takiuchi, Hitomi Nakamura, Tadashi Kimura
Scientific Reports, 2016-04-22;0(0):2045-2322.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, CF
There are currently no reviews for this product. Be the first to review Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, CF and earn rewards!
Have you used Recombinant Human VEGFR1/Flt-1 (aa 27-328) Fc Chimera, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image