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KDR
Engineered Antibody Products
Antibody-like Scaffold Protein Products
Tetramer Products
AbPlus
Recombinant Antibody Products
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Formats
Anti-KDR Recombinant Antibody Products
- 10-FnIII scaffold protein anti-Mouse Kdr (SFN-L006)
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- Scaffold Name: 10-FnIII
- Target: Kdr
- Species Reactivity: Mouse
- Derivation: Phage display
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- 10-FnIII scaffold protein anti-Human KDR (SFN-L012)
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- Scaffold Name: 10-FnIII
- Target: KDR
- Species Reactivity: Human
- Derivation: Phage display
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- 10-FnIII scaffold protein anti-Human VEGFR2 (SFN-L030)
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- Scaffold Name: 10-FnIII
- Target: VEGFR2
- Species Reactivity: Human
- Derivation: mRNA Display
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- WW domain scaffold protein anti-Human VEGFR2 (SWW-L212)
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- Scaffold Name: WW domain
- Target: VEGFR2
- Species Reactivity: Human
- Derivation: Phage display
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For Research Use Only. Not For Clinical Use.
Vascular endothelial growth factor (VEGF) is a major growth factor for endothelial cells. This gene encodes one of the two receptors of the VEGF. This receptor, known as kinase insert domain receptor, is a type III receptor tyrosine kinase. It functions as the main mediator of VEGF-induced endothelial proliferation, survival, migration, tubular morphogenesis and sprouting. The signalling and trafficking of this receptor are regulated by multiple factors, including Rab GTPase, P2Y purine nucleotide receptor, integrin alphaVbeta3, T-cell protein tyrosine phosphatase, etc.. Mutations of this gene are implicated in infantile capillary hemangiomas.
Protein class
Cancer-related genes, CD markers, Disease related genes, Enzymes, FDA approved drug targets, Human disease related genes, Metabolic proteins, Plasma proteins, RAS pathway related proteins
Predicted location
Membrane
Single cell type specificity
Group enriched (Muller glia cells, Hepatic stellate cells, Adipocytes, Endothelial cells)
Immune cell specificity
Not detected in immune cells
Cell line specificity
Group enriched (HUVEC TERT2, TIME)
Interaction
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 KDR/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 (via C-terminus domain) with ERN1 (via kinase domain); the interaction is facilitated in a XBP1 isoform 1- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (PubMed:23529610). Interacts (via juxtamembrane region) with chaperone PDCL3 (via thioredoxin fold region); the interaction leads to increased KDR/VEGFR2 abundance through inhibition of its ubiquitination and degradation (PubMed:23792958, PubMed:26059764). Interacts (tyrosine phosphorylated) with CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation of the KDR/VEGFR2 C-terminal region (PubMed:25187647). Interacts with isoform 2 of BSG (PubMed:25825981). (Microbial infection) Interacts with HIV-1 Tat.
Molecular function
Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
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