Recombinant Mouse TIE-1/Fc Chimera soluble

Biomolecules

Recombinant mouse soluble TIE-1 was fused with the Fc part of human IgG1. The recombinant mature sTIE-1/hFc is a disulfide-linked homodimeric protein. The sTIE-1/hFc monomers have a mass of approximately 105 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 130 kDa protein in SDS-PAGE under reducing conditions. The soluble receptor protein consists of the full extracellular domain (Val23-Glu749). TIE-1 (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. mouse TIE-1 cDNA encodes a 1134 amino acid (aa) residue precursor protein with an 22 residue putative signal peptide, a 733 residue extracellular domain and a 354 residue cytoplasmic domain. Whereas two ligands have been described for TIE-2 [angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2)], so far no ligand was found for TIE-1.

Since a ligand for TIE-1 has not yet been identified, the recombinant protein was not tested for biological activity.