Angiopoietin-4 Fibrinogen-like Domain (human, recombinant)

Angiopoietin-4 (ANG-4) is a member of the angiopoietin family of growth factors. It is composed of an N-terminal domain, a coiled-coil domain, and a fibrinogen-like domain, forms disulfide-linked dimers, and is the human ortholog of mouse Ang-3. ANG-4 is predominantly expressed in the lung, with lower levels of expression in the heart, liver, kidney, and other tissues. It acts as an agonist at its receptor, tunica interna endothelial cell kinase 2 (Tie2), and is involved in angiogenesis. Intratumoral protein levels of ANG-4 are increased in patients with glioblastoma. Cayman's Angiopoietin-4 Fibrinogen-like Domain (human, recombinant) protein consists of 242 amino acids and has a calculated molecular weight of 27. kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 38 kDa due to glycosylation.. Protein function: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. [The UniProt Consortium]