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Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
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KDR / VEGFR2 / FLK1
kinase insert domain receptor (a type III receptor tyrosine kinase)
Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.
Gene Name:
kinase insert domain receptor (a type III receptor tyrosine kinase)
Receptor chimeras indicate that the vascular endothelial growth factor receptor-1 (VEGFR-1) modulates mitogenic activity of VEGFR-2 in endothelial cells. Rahimi N, Dayanir V, Lashkari K. The Journal of biological chemistry. 2000 275:16986-92. (WB, IP)
[PubMed:10747927]
2
Vascular endothelial growth factor and hepatocyte growth factor levels are differentially elevated in patients with advanced retinopathy of prematurity. Lashkari K, Hirose T, Yazdany J, McMeel JW, Kazlauskas A, Rahimi N. The American journal of pathology. 2000 156:1337-44. (IHC-P; Human)
[PubMed:10751359]
[PMC:PMC1876877]
3
The carboxyl terminus controls ligand-dependent activation of VEGFR-2 and its signaling. Meyer RD, Singh AJ, Rahimi N. The Journal of biological chemistry. 2004 279:735-42. (WB, IP)
[PubMed:14573614]
[PMC:PMC1464116]
4
The carboxyl terminus of VEGFR-2 is required for PKC-mediated down-regulation. Singh AJ, Meyer RD, Band H, Rahimi N. Molecular biology of the cell. 2005 16:2106-18. (WB, IP)
[PubMed:15673613]
[PMC:PMC1073687]
5
Expression of periostin in human breast cancer. Puglisi F, Puppin C, Pegolo E, Andreetta C, Pascoletti G, D'Aurizio F, Pandolfi M, Fasola G, Piga A, Damante G, Di Loreto C. Journal of clinical pathology. 2008 61:494-8.
[PubMed:17938160]
6
Nonclinical antiangiogenesis and antitumor activities of axitinib (AG-013736), an oral, potent, and selective inhibitor of vascular endothelial growth factor receptor tyrosine kinases 1, 2, 3. Hu-Lowe DD, Zou HY, Grazzini ML, Hallin ME, Wickman GR, Amundson K, Chen JH, Rewolinski DA, Yamazaki S, Wu EY, McTigue MA, Murray BW, Kania RS, O'Connor P, Shalinsky DR, Bender SL. Clinical cancer research : an official journal of the American Association for Cancer Research. 2008 14:7272-83.
[PubMed:19010843]
7
Metabolic reprogramming by HIF-1 promotes the survival of bone marrow-derived angiogenic cells in ischemic tissue. Rey S, Luo W, Shimoda LA, Semenza GL. Blood. 2011 117:4988-98.
[PubMed:21389314]
[PMC:PMC3100705]
8
Molecular MRI differentiation of VEGF receptor-2 levels in C6 and RG2 glioma models. He T, Smith N, Saunders D, Pittman BP, Lerner M, Lightfoot S, Silasi-Mansat R, Lupu F, Towner RA. American journal of nuclear medicine and molecular imaging. 2013 3:300-11. (WB; Human)
[PubMed:23901356]
[PMC:PMC3715774]
Related Antibodies: LS-C117508.
9
Reduced Microvascular Density in Omental Biopsies of Children with Chronic Kidney Disease. Burkhardt D, Bartosova M, Schaefer B, Grabe N, Lahrmann B, Nasser H, Freise C, Schneider A, Lingnau A, Degenhardt P, Ranchin B, Sallay P, Cerkauskiene R, Malina M, Ariceta G, Schmitt CP, Querfeld U. PloS one. 2016 November;11:e0166050. (Human)[Full Text Article]
[PubMed:27846250]
[PMC:PMC5113061]
Related Antibodies: LS-C122532.
10
Zinc Finger Protein St18 Protects against Septic Death by Inhibiting VEGF-A from Macrophages. Kenta Maruyama, Hiroyasu Kidoya, Naoki Takemura, Erika Sugisawa, Osamu Takeuchi, Takeshi Kondo, Mohammed Mansour Abbas Eid, Hiroki Tanaka, Mikaël M Martino, Nobuyuki Takakura, Yasunori Takayama, Shizuo Akira, Alexis Vandenbon, Yutaro Kumagai. Cell reports. 2020 July;32:107906. [Full Text Article]
[PubMed:32668247]
11
The gene expression of human endothelial cells is modulated by subendothelial extracellular matrix proteins: short-term response to laminar shear stress. Chlupac J, Filova E, Havlikova J, Matejka R, Riedel T, Houska M, Brynda E, Pamula E, R[Character e9]my M, Bareille R, Fernandez P, Daculsi R, Bourget C, Bacakova L, Bordenave L. Tissue engineering. Part A. 2014 Aug;20:2253-64. [Full Text Article]
[PubMed:24606163]
[PMC:PMC4137337]
Related Antibodies: LS-C109100.
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PLEASE NOTE
For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.
The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).