CAPN5. a member of the calpain family of calcium-dependent cysteine proteases, plays critical roles in cellular processes such as signal transduction, apoptosis, and cytoskeletal remodeling. Unlike other calpains, CAPN5 lacks the penta-EF-hand domain required for calcium-dependent dimerization, suggesting unique regulatory mechanisms. It is expressed in various tissues, with notable activity in the retina and brain. Dysregulation of CAPN5 has been linked to pathologies, including proliferative vitreoretinopathy (PVR) and neurodegenerative disorders. CAPN5 gain-of-function mutations are specifically associated with autosomal dominant neovascular inflammatory vitreoretinopathy (ADNIV), a rare inflammatory eye disease.
CAPN5 antibodies are essential tools for studying its expression, localization, and function. Polyclonal and monoclonal antibodies targeting specific regions (e.g., catalytic domain or calcium-binding sites) enable applications like Western blotting, immunohistochemistry, and immunofluorescence. These antibodies help elucidate CAPN5’s pathological mechanisms, such as aberrant cleavage of substrates like retinal proteins or signaling molecules. Challenges in antibody development include ensuring specificity due to homology with other calpain isoforms. Recent advances in epitope mapping and recombinant protein techniques have improved antibody reliability, aiding research into CAPN5-targeted therapies for retinal and neurological diseases.