Recombinant Human RNASEK protein

RNASEK (Ribonuclease K) is a conserved endoribonuclease belonging to the RNase A superfamily, initially identified for its role in RNA metabolism and degradation. It is ubiquitously expressed in eukaryotic cells, particularly localized to endosomal and lysosomal compartments, where it contributes to RNA processing and turnover. Structurally, RNASEK contains a conserved catalytic triad (His-Lys-His) critical for its enzymatic activity, enabling cleavage of single-stranded RNA substrates.

Recent studies have linked RNASEK to innate immunity and viral defense mechanisms. It interacts with pattern recognition receptors (e.g., RIG-I-like receptors) to modulate antiviral signaling pathways, suggesting a dual role in RNA degradation and immune regulation. Additionally, RNASEK has been implicated in endocytic trafficking, where it associates with the V-ATPase complex to regulate endosomal acidification—a process essential for ligand-receptor dissociation and lysosomal function. Dysregulation of RNASEK is associated with impaired viral clearance, neurodegenerative disorders, and lysosomal storage diseases.

Recombinant RNASEK protein, typically produced in *E. coli* or mammalian expression systems, retains enzymatic activity and structural integrity for functional studies. Its applications span *in vitro* assays to dissect RNA degradation mechanisms, drug screening for antiviral therapies, and structural biology (e.g., crystallography) to elucidate substrate-binding motifs. Furthermore, recombinant RNASEK serves as a tool to investigate endosomal-lysosomal dysfunction in disease models. Despite its emerging significance, the full scope of RNASEK's biological roles and therapeutic potential remains under exploration, highlighting the need for further research into its molecular interactions and pathophysiological relevance.