|Application ||WB, IF, IHC|
|Calculated MW||150769 Da|
|Other Names||Vascular endothelial growth factor receptor 1, VEGFR-1, Fms-like tyrosine kinase 1, FLT-1, Tyrosine-protein kinase FRT, Tyrosine-protein kinase receptor FLT, FLT, Vascular permeability factor receptor, FLT1, FLT, FRT, VEGFR1|
|Target/Specificity||A synthetic peptide corresponding to residues in N-terminus of human VEGFR1 was used as immunogen. The antibody can detect both VEGFR1 and its splice isoform sFlt1.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||VEGFR-1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||FLT, FRT, VEGFR1|
|Function||Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.|
|Cellular Location||Isoform 1: Cell membrane; Single-pass type I membrane protein. Endosome. Note=Autophosphorylation promotes ubiquitination and endocytosis Isoform 3: Secreted. Isoform 5: Cytoplasm. Isoform 7: Cytoplasm.|
|Tissue Location||Detected in normal lung, but also in placenta, liver, kidney, heart and brain tissues. Specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. Isoform 2 is strongly expressed in placenta. Isoform 3 is expressed in corneal epithelial cells (at protein level). Isoform 3 is expressed in vascular smooth muscle cells (VSMC).|
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Provided below are standard protocols that you may find useful for product applications.
VEGFR-1 (vascular endothelial growth factor receptor 1) is a 180-kDa membrane receptor tyrosine kinase that is the receptor for vascular endothelial growth factor (VEGF), VEGFB and PGF. VEGF is a key regulator of physiological angiogenesis during embryogenesis, skeletal growth and reproductive functions. VEGF has also been implicated in pathological angiogenesis associated with tumors, intraocular neovascular disorders and other conditions (1). VEGFR-1 has seven extracellular Ig-like domains; the second domain from the N-terminus is necessary and sufficient for high affinity VEGF binding (2). The biological effects of VEGF are mediated by VEGFR-1 and VEGFR-2 (1), and two major tyrosine phosphorylation sites at Tyr 1213 and Tyr 1242 and two minor tyrosine phosphorylation sites at Tyr 1327 and Tyr 1333 exist in VEGFR-1 (3).
1. Ferrara, N. et al. The biology of VEGF and its receptors. Nat. Med. 9: 669
2. Starovasnik, M.A., et al. Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states. J Mol Biol. 293: 531
3. Ito, N., et al. Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules. J Biol Chem. 273: 23410
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