|Detection of Mouse Angiopoietin‑1 by Western Blot. Western blot shows lysates of mouse heart tissue and mouse kidney tissue. PVDF membrane was probed with 2 µg/mL of Rat Anti-Mouse Angiopoietin‑1 Monoclonal Antibody (Catalog # MAB8220) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Angiopoietin‑1 at approximately 75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Angiopoietin-1 (Ang-1) and Angiopoietin-2 (Ang-2) are two closely related secreted ligands which bind with similar affinity to Tie-2, a receptor tyrosine kinase with immunoglobulin and epidermal growth factor homology domains expressed primarily on endothelial cells and early hematopoietic cells. Tie-2 and angiopoietins have been shown to play critical roles in embryogenic angiogenesis and in maintaining the integrity of the adult vasculature (1).
Ang-1 cDNA encodes a 498 amino acid (aa) residue precursor protein that contains a coiled-coiled domain near the amino-terminus and a fibrinogen-like domain at the C-terminus. Human Ang-1 shares approximately 97% and 60% amino acid sequence identity with mouse Ang-1 and human Ang-2, respectively (1, 2). Ang-1 activates Tie-2 signaling on endothelial cells to promote chemotaxis, cell survival, cell sprouting, vessel growth and stabilization (1, 3, 4). Ang-2 has alternatively been reported to be an antagonist for Ang-1 induced Tie-2 signaling as well as an agonist for Tie-2 signaling, depending on the cell context (5).
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