C6ORF108 encodes a protein that is involved in several biochemical functions. The gene produces two alternative transcripts encoding different proteins. The recombinant form of this protein is typically produced in Escherichia coli (E. coli) and is often tagged with a His-tag for purification purposes . The recombinant protein consists of 194 amino acids, including a 20 amino acid His-tag at the N-terminus, and has a molecular mass of approximately 21.2 kDa .
The exact function of C6ORF108 is not fully understood. However, studies in rats suggest that it plays a role in cellular proliferation and c-Myc-mediated transformation . The protein has been shown to catalyze the cleavage of the N-glycosidic bond of deoxyribonucleoside 5’-monophosphates, yielding deoxyribose 5-phosphate and a purine or pyrimidine base . This activity suggests a role in nucleotide metabolism and DNA repair processes.
C6ORF108 is involved in several pathways and interacts with various proteins and molecules. These interactions have been detected through methods such as yeast two-hybrid, co-immunoprecipitation, and pull-down assays . Some of the proteins that interact with C6ORF108 include TERF1, FTSJ1, POT1, PILRA, and BRCA1 . These interactions indicate that C6ORF108 may have a broader role in cellular processes beyond its enzymatic activity.
Recombinant C6ORF108 is used in various research applications, including studies on gene expression regulation, protein-protein interactions, and cellular signaling pathways. The availability of recombinant C6ORF108 allows researchers to investigate its function and mechanism in a controlled environment, providing insights into its role in human health and disease .