Tyrosine kinase with immunoglobulin-like and EGF-like domains 1 (TIE-1) is a tyrosine kinase cell-surface receptor that is expressed primarily in endothelial cells. It exhibits high homology to TEK/TIE-2 and inhibits the binding of TEK/TIE-2 to the growth factor angiopoietin-1. The extracellular domain of TIE-1 can be cleaved by multiple factors, including vascular endothelial growth factor (VEGF); this results in loss of its ability to inhibit TEK/TIE-2. In addition to its role in angiogenesis, TIE-1 is reported to have proinflammatory effects in endothelial cells. TIE-1 is also known as tyrosine-protein kinase receptor Tie-1, TIE, and JTK14.
These products are affinity-purified IgG antibodies that recognize human TIE-1 protein. The antibodies were raised in rabbit or mouse using recombinant protein or a synthetic peptide and can be used for Western blot (WB) detection, immunohistochemical (IHC) detection, immunoprecipitation (IP), or flow cytometry (FCM) of human TIE-1 protein.