TDG Polyclonal Antibody

Thymine DNA Glycosylase (TDG) is a nuclear protein that belongs to the TDG/mug DNA glycosylase family. TDG amends G/T mismatches to G/C pairs by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired thymine. In addition, TDG amends a subset of G/U mispairs inefficiently removed by the more abundant uracil glycosylases. Retinoic acid receptors interact with TDG physically and functionally, improving the capability of the retinoid X receptor and the retinoid X receptor/retinoid acid receptor complex to bind to their response elements. This protein's DNA substrate and AP site binding affinity is diminished when it interacts with SUMO-1 and SUMO-2/3, two ubiquitin-like proteins that also covalently modify TDG. This sumoylation correlates with a substantial rise in enzymatic turnover in reactions with a G/U substrate and the shortage of G/T processing activity.