Recombinant Human APOLD1 protein

APOLD1 (Apolipoprotein L Domain-Containing Protein 1) is a secreted glycoprotein encoded by the APOLD1 gene, primarily expressed in vascular endothelial cells and smooth muscle cells. First identified in 2003. it plays a regulatory role in vascular function and hemodynamic responses. The protein contains an N-terminal apolipoprotein L-like domain and a C-terminal disordered region, suggesting involvement in lipid metabolism and cell signaling. APOLD1 is dynamically regulated by mechanical forces like shear stress, linking it to blood flow adaptation and vascular remodeling processes.

Recombinant APOLD1 protein is typically produced using mammalian expression systems (e.g., HEK293 cells) to ensure proper post-translational modifications, including glycosylation. Purification often involves affinity tags like His-tag for standardized isolation. Its primary research applications focus on elucidating vascular biology mechanisms, particularly endothelial barrier function, angiogenesis, and inflammatory responses. Studies suggest APOLD1 interacts with integrins and modulates VEGF signaling pathways, making it relevant to atherosclerosis, hypertension, and tumor vascularization research. Recent investigations also explore its potential as a biomarker for cardiovascular diseases and its role in endoplasmic reticulum stress responses. The recombinant protein serves as a critical tool for in vitro assays studying endothelial cell behavior under flow conditions and for developing therapeutic strategies targeting vascular pathologies.