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Description
Rabbit Anti-Human TDG polyclonal antibody for WB, ICC. G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.29; UniProt Q13569; also known as hTDG, Thymine-DNA glycosylase) is encoded by the TDG gene (Gene ID 6996) in human. Base excision repair (BER) is initiated by damage-specific DNA glycosylases that recognize and remove aberrant bases by hydrolyzing the N-glycosidic bond, creating an apurinic/apyrimidinic (AP) site. This is followed by an (AP)-endonuclease-catalyzed DNA strand incision 5? to the AP site, trimming of the 5? end by an (AP)-lyase or an endonuclease, DNA resynthesis by a DNA polymerase and strand sealing by a DNA ligase. Monofunctional glycosylases have only glycosylase activity, whereas bifunctional glycosylases possess additional AP lyase activity and can therefore convert a base lesion into a single-strand break without the need for a separate AP endonuclease. TDG is a monofunctional DNA glycosylase that excises thymine and uracil from G·T and G·U mismatched oligonucleotide substrates as well as the highly mutagenic adduct 3,N4-ethenocytosine from double-stranded DNA. TDG DNA-binding affinity is regulated by SUMOylation, which dramatically reduces its affinity toward DNA substrate and AP site. Sumoylation also potentiates the stimulatory effect of (AP)-endonuclease (APE1/HAP1) on TDG.
Immunogen
KLH-conjugated linear peptide corresponding to a sequence from the N-terminal region of human Thymine-DNA Glycosylase.