Recombinant Human LDB3 protein

LDB3 (LIM domain-binding protein 3), also known as Cypher or ZASP, is a striated muscle-specific protein crucial for maintaining structural integrity and functional regulation of the sarcomere, the basic contractile unit of muscle cells. It belongs to the PDZ-LIM protein family, characterized by an N-terminal PDZ domain and one or three C-terminal LIM domains, depending on alternative splicing. The PDZ domain facilitates interactions with cytoskeletal proteins like α-actinin and myotilin, while the LIM domains mediate protein-protein interactions involved in signaling pathways.

LDB3 plays a vital role in anchoring and stabilizing the Z-discs of sarcomeres, ensuring proper force transmission during muscle contraction. Mutations in the LDB3 gene are linked to human cardiomyopathies (e.g., dilated cardiomyopathy) and skeletal myopathies (e.g., ZASP-related myopathy), often associated with Z-disc disintegration and impaired contractility. Recombinant LDB3 proteins are engineered to study these pathogenic mechanisms, typically expressed in bacterial (e.g., E. coli) or mammalian systems for structural and functional analyses.

Research applications include investigating LDB3’s interaction networks, post-translational modifications, and the impact of disease-associated mutations. Recombinant variants (wild-type or mutant) are used in biochemical assays, cell culture models, and animal studies to explore therapeutic strategies targeting sarcomere stability. Additionally, they serve as antigens for antibody development in diagnostic tools. Understanding LDB3’s molecular roles through recombinant proteins offers insights into muscle pathophysiology and potential interventions for cardiac and muscular disorders.