VEGFR-3/FLT-4/Fc Chimera, soluble

Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774) . All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis.