Tetranectin (TN), also known as C-type lectin domain family 3 member B (CLEC3B), is a plasminogen-binding protein belonging to the C-type lectin superfamily. It is primarily secreted into the extracellular matrix and plays roles in fibrinolysis, tissue remodeling, and lipid metabolism. Structurally, Tetranectin forms homotrimers with a carbohydrate-recognition domain (CRD) that mediates interactions with plasminogen and lipoprotein particles, influencing proteolytic and metabolic pathways.
Antibodies targeting Tetranectin are valuable tools for studying its expression, localization, and function in physiological and pathological contexts. In research, Tetranectin antibodies are used in techniques like Western blotting, immunohistochemistry (IHC), and ELISA to quantify protein levels in tissues or biofluids. Studies have linked altered Tetranectin expression to diseases such as cancer (e.g., reduced levels in breast, liver, and lung cancers), neurological disorders (e.g., Alzheimer’s disease), and cardiovascular conditions. Its potential role as a biomarker for disease progression or prognosis is an active area of investigation.
Notably, Tetranectin antibodies aid in elucidating its interaction networks, including binding partners like apolipoprotein A-I and components of the plasminogen activation system. Commercial antibodies are typically raised against specific epitopes, such as the N-terminal or CRD regions, and validated for cross-reactivity across species (e.g., human, mouse). Ongoing research explores therapeutic applications, such as modulating Tetranectin to influence fibrinolysis or lipid metabolism in metabolic syndromes.