VEGF R1/Flt-1 Fc Chimera (aa27-328), Human

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Vascular endothelial growth factor receptor 1 (VEGF R1) , also known as FMS-like tyrosine kinase (Flt1), is a receptor tyrosine kinase which plays a critical role in angiogenesis. Human VEGF R1 contains a signal peptide (aa 1-22), an extracellular domain (ECD aa 27-758) with seven Ig-like repeats, a trans-membrane domain (aa 759-780) and a cytoplasmic region (aa 781-1338) with a tyrosine kinase domain and several autocatalytic phosphotyrosine sites. VEGFR-1 and VEGFR-2 are closely related receptor tyrosine kinases and have both common and specific ligands. VEGFR-1 is a kinase-impaired RTK whereas VEGFR-2 is a highly active kinase. Vascular endothelial growth factors (VEGFs) are crucial regulators of vascular development during embryogenesis (vasculogenesis) as well as blood-vessel formation (angiogenesis) in the adult. In mammals, five VEGF ligands, which occur in several different splice variants and processed forms, have been identified so far. These ligands bind in an overlapping pattern to VEGF receptor-1, -2 and -3 (VEGFR1-3), as well as to co-receptors (here defined as VEGF-binding molecules that lack established VEGF-induced catalytic function), such as heparin sulphate proteoglycans (HSPGs) and neuropilins.
Recombinant Human VEGF R1 produced in CHO cells is a polypeptide chain containing 535 amino acids. rhVEGF R1 has a molecular mass of 80 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.