Recombinant Human DNAH11 protein

DNAH11 (Dynein Axonemal Heavy Chain 11) is a member of the dynein motor protein family, which plays a critical role in the movement of cilia and flagella. This large cytoplasmic protein is a key component of the axonemal dynein complex, providing mechanical force for ciliary beating through ATP hydrolysis. Structurally, DNAH11 contains a conserved N-terminal motor domain, a central helical stalk, and a C-terminal microtubule-binding domain. Its function is essential for mucociliary clearance in the respiratory tract, embryonic nodal cilia signaling, and sperm motility.

Recombinant DNAH11 protein refers to the engineered form of this protein produced using heterologous expression systems, such as bacterial (e.g., E. coli) or mammalian cell cultures. This biotechnology approach allows researchers to obtain purified DNAH11 for functional studies, antibody production, and structural analysis. The recombinant form typically preserves functional domains while enabling site-specific modifications for mechanistic investigations. Researchers often clone specific DNAH11 variants associated with diseases to study their biophysical properties and interactions.

Mutations in DNAH11 are linked to primary ciliary dyskinesia (PCD), a genetic disorder characterized by chronic respiratory infections, laterality defects, and infertility. Interestingly, DNAH11-associated PCD often presents with normal ciliary ultrastructure, complicating diagnosis. Beyond ciliopathies, aberrant DNAH11 expression has been observed in various cancers, where it may influence cell migration and metastasis. Recombinant DNAH11 proteins facilitate the development of diagnostic assays and therapeutic strategies, including gene therapy approaches for PCD. Current research focuses on understanding how specific mutations disrupt dynein ATPase activity and microtubule sliding mechanics, aiming to establish genotype-phenotype correlations and identify potential therapeutic targets.