Synemin, also known as desmuslin, is an intermediate filament (IF) protein belonging to the type III IF family, which includes desmin, vimentin, and glial fibrillary acidic protein (GFAP). First identified in the 1980s, synemin is expressed in muscle cells (skeletal, cardiac, and smooth) and certain glial cells. It plays a critical role in maintaining cellular structural integrity by linking IF networks to other cytoskeletal components, such as actin microfilaments and microtubules, through interactions with α-actinin, dystrophin, and vinculin. Synemin exists as two major isoforms, α-synemin (∼180 kDa) and γ-synemin (∼150 kDa), generated via alternative splicing. These isoforms exhibit tissue-specific expression patterns, with α-synemin predominant in muscle and γ-synemin in neural and muscle tissues.
Synemin antibodies are widely used in research to study its involvement in cellular mechanotransduction, muscle contraction, and cell migration. Dysregulation of synemin has been implicated in muscular dystrophies, cardiomyopathies, and cancer metastasis. In disease models, synemin deficiency disrupts IF network organization, impairing cell adhesion and mechanical resilience. Antibodies targeting synemin (e.g., monoclonal clones like SYNM/4H8) enable detection via Western blot, immunofluorescence, and immunohistochemistry, aiding investigations into its role in cytoskeletal dynamics and pathology. Its dual role as a structural scaffold and signaling mediator makes synemin a biomarker of interest in neuromuscular and oncological studies.