Recombinant Human ANG1 protein

Angiopoietin-1 (ANG1) is a key secretory glycoprotein belonging to the angiopoietin family, primarily involved in vascular development, maturation, and stability. It binds to the Tie2 receptor tyrosine kinase on endothelial cells, triggering signaling pathways that promote vessel remodeling, reduce vascular permeability, and suppress inflammation. Unlike VEGF, which drives early angiogenesis, ANG1 stabilizes nascent vasculature by enhancing endothelial cell survival and cell-matrix adhesion. Its role in maintaining vascular integrity has made it a therapeutic target for conditions involving vascular dysfunction, such as ischemic diseases, diabetic retinopathy, and sepsis.

Recombinant ANG1 protein is engineered using biotechnological methods, often via mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, though bacterial or yeast systems are also employed for cost efficiency. The recombinant form typically retains functional domains, including the coiled-coil and fibrinogen-like domains critical for receptor binding and oligomerization. To enhance stability and solubility, truncated variants (e.g., COMP-ANG1) or fusion tags (e.g., Fc tags) are commonly incorporated.

Preclinical studies highlight its therapeutic potential: in myocardial infarction models, ANG1 improves cardiac function by enhancing collateral circulation; in neurodegenerative diseases, it stabilizes the blood-brain barrier. Additionally, it synergizes with VEGF to promote non-leaky vascular networks in tissue engineering. Challenges include optimizing delivery methods (viral vectors, hydrogels) and balancing pro-angiogenic versus stabilizing effects in cancer contexts. Current research focuses on clinical translation, leveraging ANG1’s dual role in vascular repair and anti-inflammatory signaling to address complex pathologies.