Blockade of Receptor-ligand Interaction
|Angiopoietin-2 binding to Tie-2 blocked by Zebrafish Tie-2 Antibody. In a functional ELISA, Recombinant Human Angiopoietin-2 (Catalog # 623-AN) binds to immobilized Recombinant Zebrafish Tie-2 Fc Chimera (Catalog # 928‑T2) coated at 4 µg/mL (100 µL/well) in a dose-dependent manner (orange line). Binding is blocked (green line) by increasing concentrations of Mouse Anti-Zebrafish Tie-2 Monoclonal Antibody (Catalog # MAB928). At 0.5 μg/mL, this antibody will block 90% of the binding.|
Tie-1/Tie (tyrosine kinase with Ig and EGF homology domains 1) and Tie-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis.
Zebrafish Tie-2 cDNA encodes a 1116 amino acid (aa) residue precursor protein shares 38% sequence homology with human Tie-2 in the extracellular domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind Tie-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-2 display similar angiogenesis defects.
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