SERPINE2. also known as protease nexin-1 (PN-1), is a serine protease inhibitor involved in regulating extracellular matrix remodeling, coagulation, and cellular signaling. It primarily inhibits proteases like thrombin, plasmin, and urokinase-type plasminogen activator (uPA), modulating processes such as fibrinolysis, angiogenesis, and tissue repair. Expressed in various tissues, including the brain, vascular endothelium, and secretory organs, SERPINE2 plays roles in both physiological and pathological conditions, such as fibrosis, cancer progression, and neurodegenerative diseases.
SERPINE2 antibodies are immunological tools used to detect and quantify SERPINE2 protein expression in research settings. These antibodies aid in studying its involvement in diseases like prostate cancer, chronic obstructive pulmonary disease (COPD), and Alzheimer's disease, where dysregulated SERPINE2 expression correlates with tumor metastasis, tissue fibrosis, or neuronal dysfunction. Researchers utilize SERPINE2 antibodies in techniques like Western blotting, immunohistochemistry, and ELISA to explore its localization, interaction partners, and mechanistic pathways.
Interest in SERPINE2 stems from its dual role as a potential biomarker and therapeutic target. For example, elevated SERPINE2 levels in tumors may indicate poor prognosis, while its inhibition could mitigate fibrosis or thrombosis. However, its complex regulation and context-dependent functions require further investigation. SERPINE2 antibodies thus serve as critical reagents for advancing our understanding of its biology and translational applications in precision medicine.