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VEGFR2/Flk-1/CD309/KDR Protein, Antibody, ELISA Kit, cDNA Clone

Human VEGFR2/Flk-1/CD309/KDR Protein

Description: Active
Expression host: Human Cells
  • Slide 1
10012-H02H-50
10012-H02H-100
50 µg / $170
100 µg / $290
Add to Cart
Description: Active
Expression host: Human Cells
  • Slide 1
10012-H08H-50
10012-H08H-100
50 µg / $210
100 µg / $290
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Expression host: Baculovirus-Insect Cells
  • Slide 1
  • Slide 1
10012-H20B1-50
10012-H20B1-100
50 µg / $180
100 µg / $290
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Mouse VEGFR2/Flk-1/CD309/KDR Protein

Expression host: Human Cells
  • Slide 1
50998-M08H-50
50998-M08H-100
50 µg / $170
100 µg / $290
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Expression host: Human Cells
  • Slide 1
50998-M02H-50
50998-M02H-100
50 µg / $180
100 µg / $290
Add to Cart

Rat VEGFR2/Flk-1/CD309/KDR Protein

Expression host: Human Cells
  • Slide 1
80113-R02H-50
80113-R02H-100
50 µg / $170
100 µg / $290
Add to Cart
Expression host: Human Cells
  • Slide 1
80113-R08H-20
80113-R08H-50
20 µg / $140
50 µg / $290
Add to Cart

VEGFR2/Flk-1/CD309/KDR Related Areas

VEGFR2/Flk-1/CD309/KDR Related Pathways

VEGFR2/Flk-1/CD309/KDR Related Product

VEGFR2/Flk-1/CD309/KDR Summary & Protein Information

VEGFR2/Flk-1/CD309/KDR Related Information

VEGFR2/Flk-1/CD309/KDR Background

Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation: Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by the small molecule PTK inhibitor SU5614 ((3Z)-5-Chloro-3-[(3,5-dimethyl-1H-pyrrol-2-yl)methylene]-1,3- dihydro-2H-indol-2-one). May be regulated by hydrogen sulfide (H(2)S) levels via a H(2)S-sensitive intracellular disulfide bond.
Subunit structure: Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6. Interacts with HIV-1 Tat.
Domain: The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.
Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Cytoplasm. Nucleus. Cytoplasmic vesicle. Early endosome. Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus.
Isoform 2: Secreted (Probable).
Isoform 3: Secreted.
Tissue specificity: Detected in cornea (at protein level). Widely expressed.
Post-translational: N-glycosylated.
Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases.
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-951 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1175 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1214 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-951, Tyr-996, Tyr-1054, Tyr-1059, Tyr-1175 and Tyr-1214.
The inhibitory disulfide bond between Cys-1024 and Cys-1045 may serve as a specific molecular switch for H(2)S-induced modification that regulates VEGFR2 function.
Involvement in disease: Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
Note=Plays a major role in tumor angiogenesis. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.
Contains 7 Ig-like C2-type (immunoglobulin-like) domains.
Contains 1 protein kinase domain.C
General information above from UniProt

VEGFR2, also called as KDR or Flk-1, is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo. VEGFR2 was shown to be the primary signal transducer for angiogenesis and the development of pathological conditions such as cancer and diabetic retinopathy. It has been shown that VEGFR2 is expressed mainly in the endothelial cells, and the expression is upregulated in the tumor vasculature. Thus the inhibition of VEGFR2 activity and its downstream signaling are important targets for the treatment of diseases involving angiogenesis. VEGFR2 transduces the major signals for angiogenesis via its strong tyrosine kinase activity. However, unlike other representative tyrosine kinase receptors, VEGFR2 does not use the Ras pathway as a major downstream signaling but rather uses the phospholipase C-protein kinase C pathway to signal mitogen-activated protein (MAP)-kinase activation and DNA synthesis. VEGFR2 is a direct and major signal transducer for pathological angiogenesis, including cancer and diabetic retinopathy, in cooperation with many other signaling partners; thus, VEGFR2 and its downstream signaling appear to be critical targets for the suppression of these diseases. VEGF and VEGFR2-mediated survival signaling is critical to endothelial cell survival, maintenance of the vasculature and alveolar structure and regeneration of lung tissue. Reduced VEGF and VEGFR2 expression in emphysematous lungs has been linked to increased endothelial cell death and vascular regression.

VEGFR2/Flk-1/CD309/KDR Alternative Name

VEGFR2/Flk-1/CD309/KDR Related Studies

  • Shibuya M. (2006) Vascular endothelial growth factor (VEGF)-Receptor2: its biological functions, major signaling pathway, and specific ligand VEGF-E. Endothelium. 13(2): 63-9.
  • Marwick JA, et al. (2010) Cigarette smoke regulates VEGFR2-mediated survival signaling in rat lungs. J Inflamm (Lond). 7(1): 11.
  • Bruns AF, et al. (2010) Ligand-stimulated VEGFR2 signaling is regulated by co-ordinated trafficking and proteolysis. Traffic. 11(1): 161-74.
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