Recombinant Human C12orf66 Protein

The human C12orf66 protein, encoded by the open reading frame 66 on chromosome 12. remains poorly characterized, with limited functional data available in current literature. While its exact biological role is unclear, bioinformatic analyses suggest it may function as a nucleic acid-binding protein, potentially involved in RNA metabolism or regulation. Structural predictions indicate conserved motifs resembling those in RNA-processing enzymes, though experimental validation is lacking. Some studies associate C12orf66 with cellular stress responses, as its expression appears modulated under oxidative or hypoxic conditions. Notably, its recombinant form (expressed in Escherichia coli or mammalian systems) has been utilized in preliminary biochemical studies, revealing weak ATPase activity and nucleic acid interaction capabilities in vitro. Emerging evidence links C12orf66 to antiviral immunity, with RNA-seq data showing upregulated expression during viral infections, though mechanistic insights remain speculative. The protein's subcellular localization appears predominantly cytoplasmic, as demonstrated by fluorescence-tagged versions in cell models. Despite being evolutionarily conserved in vertebrates, no direct disease associations have been confirmed, though genomic variations in C12orf66 were sporadically reported in cancer sequencing databases. Current research focuses on identifying interaction partners and pathway associations using affinity purification-mass spectrometry approaches. Its recombinant version continues to serve as a tool for antibody development and functional screening platforms, emphasizing the need for deeper molecular characterization to elucidate its physiological significance.