Recombinant Human SVEP1 protein

SVEP1 (Sushi, von Willebrand factor type A, EGF, and pentraxin domain-containing protein 1), also known as polydom, is a large extracellular matrix glycoprotein implicated in cell adhesion, signaling, and tissue development. Structurally, it contains multiple conserved domains, including sushi repeats, von Willebrand factor type A (vWA) domains, epidermal growth factor (EGF)-like motifs, and a C-terminal pentraxin domain, which collectively mediate interactions with integrins and other extracellular components. SVEP1 is broadly expressed in tissues such as blood vessels, bone, and cartilage, and plays critical roles in embryonic development, particularly in cardiovascular and skeletal systems.

Functionally, SVEP1 interacts with integrin α9β1. modulating cellular processes like adhesion, migration, and proliferation. It regulates vascular smooth muscle cell behavior and arterial stiffness, linking it to cardiovascular pathologies. Studies also associate SVEP1 variants with coronary artery disease, hypertension, and osteoporosis. Intriguingly, SVEP1 exhibits dual roles in cancer, acting as a tumor suppressor by inhibiting angiogenesis in some contexts or promoting metastasis in others, depending on the tumor microenvironment.

Recombinant SVEP1 protein is typically produced in mammalian or insect cell systems to preserve post-translational modifications (e.g., glycosylation) essential for its biological activity. This engineered protein serves as a vital tool for studying SVEP1-dependent signaling pathways, structural interactions, and its therapeutic potential. Current research focuses on elucidating its role in disease mechanisms, developing diagnostic biomarkers, and exploring targeted therapies for cardiovascular disorders and cancer. Its multifunctional nature and disease associations make SVEP1 a compelling subject for translational research.