Dysferlin, also known as Romeo, is a large transmembrane protein encoded by the *DYSF* gene, primarily expressed in skeletal muscle and involved in membrane repair processes. It plays a critical role in resealing sarcolemmal disruptions by mediating vesicle fusion and membrane patching. Mutations in *DYSF* are linked to muscular dystrophies, including limb-girdle muscular dystrophy type 2B (LGMD2B) and Miyoshi myopathy, characterized by progressive muscle weakness and degeneration. Dysferlin-deficient models show impaired membrane repair, highlighting its functional importance.
The Dysferlin (Romeo) antibody is a key tool for studying these disorders. It specifically targets dysferlin epitopes, enabling detection in Western blot, immunohistochemistry, or immunofluorescence. Researchers use it to assess dysferlin expression levels in muscle biopsies, aiding diagnosis and differentiation from other dystrophies with overlapping symptoms. Commercially available monoclonal and polyclonal antibodies vary in specificity, requiring validation for experimental consistency.
Recent studies explore dysferlin's interactions with other proteins (e.g., caveolin-3. annexins) and its role in autophagy and inflammation. Therapeutic strategies, including gene therapy and exon-skipping, aim to restore dysferlin function. The antibody remains vital for preclinical testing of such therapies. Despite challenges in detecting full-length dysferlin due to its size (~230 kDa) and post-translational modifications, optimized protocols ensure reliable results, advancing both mechanistic understanding and translational research.