Nesprin1 (nuclear envelope spectrin repeat protein 1), also known as SYNE1. is a key component of the LINC (linker of nucleoskeleton and cytoskeleton) complex, which bridges the nuclear envelope and connects the nuclear lamina to the cytoskeleton. It plays a critical role in maintaining nuclear structure, positioning, and mechanical signaling by anchoring the nucleus to actin filaments via its C-terminal KASH domain. Nesprin1 is highly expressed in muscle and neuronal tissues, where its function is vital for cellular integrity and mechanotransduction.
Antibodies targeting Nesprin1 are essential tools for studying its expression, localization, and interactions in cellular and disease models. They are widely used in techniques like immunofluorescence, Western blotting, and immunoprecipitation to explore Nesprin1's involvement in nuclear envelope stability, cell migration, and differentiation. Dysregulation or mutations in Nesprin1 are linked to muscular dystrophies (e.g., Emery-Dreifuss muscular dystrophy), cardiomyopathies, and neurological disorders, making these antibodies valuable in both basic research and clinical diagnostics.
Most Nesprin1 antibodies are raised against specific epitopes, such as its N-terminal spectrin repeats or C-terminal KASH domain, enabling isoform-specific detection. Validation often includes cross-reactivity checks across species (human, mouse, rat) and confirmation of specificity using knockout controls. Researchers rely on these antibodies to elucidate Nesprin1's role in cellular mechanobiology and its pathological implications, advancing insights into nuclear-cytoskeletal coupling mechanisms.