Legumain, also known as asparaginyl endopeptidase (AEP) or LGMN, is a cysteine protease that primarily localizes to lysosomes and endosomes. It plays a critical role in protein processing, including the cleavage of substrates at asparagine or aspartic acid residues. Initially studied for its involvement in antigen processing for MHC class II presentation, legumain has gained attention for its diverse roles in pathological conditions such as cancer, neurodegenerative diseases, and inflammation. In cancer, legumain is often overexpressed in tumor tissues and the tumor microenvironment, contributing to extracellular matrix remodeling, invasion, and metastasis. Its dysregulation is also linked to Alzheimer’s disease, where it may process amyloid precursor proteins.
Legumain-specific antibodies are essential tools for studying its expression, localization, and function. These antibodies enable detection via techniques like Western blotting, immunohistochemistry, and flow cytometry. Monoclonal antibodies, known for high specificity, are widely used to target distinct epitopes, while polyclonal antibodies may offer broader detection across species. Research applications include exploring legumain’s role as a biomarker for disease progression or as a therapeutic target. Recent studies also investigate legumain-activated prodrugs, highlighting its potential in targeted cancer therapies. Validating antibody specificity remains crucial due to structural similarities among cysteine proteases. Overall, legumain antibodies are pivotal in advancing understanding of its biological and pathological significance. (298 words)