Introducing the recombinant human ATP-dependent DNA helicase DDX11 fragment (residues 198-515), a highly stable and soluble protein unit ideal for structural and biochemical studies. This 318-amino acid fragment retains key functional attributes of the full-length enzyme, offering researchers a reliable tool for investigating DNA replication, repair mechanisms, and genomic stability processes.

ATP-dependent DNA helicase DDX11 is a crucial human enzyme involved in multiple aspects of genomic maintenance, including DNA replication, DNA repair, heterochromatin organization, and ribosomal RNA synthesis. The full-length protein functions as both a DNA-dependent ATPase and ATP-dependent DNA helicase, capable of unwinding DNA duplexes up to 500 bp with the assistance of replication protein A or the Ctf18-RFC complex. It plays essential roles in DNA double-strand break repair at replication forks, sister chromatid cohesion regulation, and mitotic chromosome segregation. DDX11 localizes primarily to the nucleus and nucleolus, with additional presence at spindle poles, centrosomes, and the midbody during mitosis. Its involvement in fundamental cellular processes makes it a protein of significant interest for cancer research, developmental biology, and genomic stability studies.