Recombinant Human DHX33 protein

**Background of DHX33 Recombinant Protein**

DHX33. a member of the DEAH-box helicase family, is an ATP-dependent RNA helicase involved in diverse cellular processes, including transcription, RNA splicing, translation, and innate immune responses. It plays critical roles in unwinding double-stranded RNA (dsRNA) or RNA-DNA hybrids, facilitating RNA metabolism and genomic stability. DHX33 is ubiquitously expressed and implicated in cell proliferation, apoptosis, and viral defense mechanisms. Dysregulation of DHX33 has been linked to cancers, neurodevelopmental disorders, and immune-related diseases, underscoring its biological significance.

Recombinant DHX33 protein is engineered through molecular cloning and heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functional form of the enzyme. The protein typically retains conserved structural domains: an N-terminal domain for substrate recognition, a DEAH catalytic core for ATP hydrolysis, and a helicase domain for RNA binding and unwinding. These features enable its application in *in vitro* studies to dissect RNA helicase mechanisms, protein-RNA/DNA interactions, and nucleic acid remodeling processes.

Research utilizing DHX33 recombinant protein has advanced understanding of its role in stress granule formation, ribosome biogenesis, and antiviral signaling (e.g., via RIG-I-like receptor pathways). Additionally, it serves as a tool for screening small-molecule inhibitors targeting helicase activity in cancer or inflammation. In disease models, DHX33 has been shown to influence tumor progression by modulating oncogene expression and viral replication cycles, positioning it as a potential therapeutic target. Overall, DHX33 recombinant protein is pivotal for elucidating helicase-driven cellular mechanisms and developing targeted interventions in human diseases.