Recombinant Human DNA-binding protein SMUBP-2 fragment (residues 891-993) is a highly purified protein product derived from the IGHMBP2 gene. This 103-amino acid fragment represents a stable and soluble unit of the full-length protein, which functions as an ATP-dependent helicase involved in RNA and DNA unwinding. This carefully selected fragment is ideal for structural studies, biochemical characterization, and functional assays.

The full-length DNA-binding protein SMUBP-2 (also known as IGHMBP2) is a multifunctional enzyme with both 5' to 3' helicase activity (EC 3.6.4.12 and EC 3.6.4.13) that unwinds RNA and DNA duplexes in an ATP-dependent manner. This protein demonstrates specificity for 5'-phosphorylated single-stranded guanine-rich sequences and plays crucial roles in RNA metabolism, ribosome biogenesis, and potentially translation initiation. SMUBP-2 also interacts with tRNA-Tyr and may participate in transcriptional regulation. The protein localizes to both nuclear and cytoplasmic compartments, with evidence of presence in axonal projections, suggesting diverse cellular functions across different subcellular environments.