LMLN (lysosomal membrane protein 2-like) is a transmembrane protein predominantly localized in lysosomal and endosomal compartments. It shares structural homology with lysosomal-associated membrane proteins (LAMPs) and is implicated in intracellular vesicle trafficking, lysosomal function, and autophagy. LMLN's role in maintaining lysosomal integrity and regulating cargo sorting has drawn attention in studies of neurodegenerative diseases, cancer, and metabolic disorders, where lysosomal dysfunction is a hallmark.
Antibodies targeting LMLN are valuable tools for investigating its expression, localization, and interaction networks. They enable detection via techniques like Western blotting, immunofluorescence, and immunohistochemistry, aiding in the exploration of LMLN's involvement in pathological processes. For instance, altered LMLN expression has been linked to tumor progression and chemoresistance in certain cancers, suggesting its potential as a biomarker or therapeutic target.
Recent research also highlights LMLN's interaction with autophagy-related proteins, underscoring its significance in cellular stress responses. However, the functional complexity of LMLN and its splice variants necessitates highly specific antibodies to avoid cross-reactivity. As interest in lysosome-centric pathways grows, LMLN antibodies remain critical for deciphering its biological and pathological mechanisms, offering insights into novel therapeutic strategies for lysosome-related diseases.