Recombinant Human TDG protein (denatured) (His tag N-Terminus)
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Recombinant Human TDG protein (denatured) (His tag N-Terminus) is a Human Full Length protein, in the 1 to 410 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
G/T mismatch-specific thymine DNA glycosylase, Thymine-DNA glycosylase, hTDG, TDG
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TDG protein (denatured) (His tag N-Terminus) (AB134525)
15% SDS-PAGE analysis of 3 μg ab134525.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Thymine DNA glycosylase is involved in the active DNA demethylation process. It participates in the DNA repair machinery as part of the base excision repair complex interacting with other proteins involved in this pathway. TDG's function guarantees the correct removal and replacement of erroneous bases which might otherwise result in mutations or faulty gene expression. This activity is tightly regulated to ensure accurate DNA maintenance and cellular function.
Pathways
TDG functions within the base excision repair and DNA demethylation pathways. In these pathways proteins such as APE1 (apurinic/apyrimidinic endodeoxyribonuclease 1) work closely with TDG to process intermediates generated during base removal. Through base excision repair TDG contributes to the protection against mutations by correcting base mispairings. The DNA demethylation pathway in which TDG participates also plays a role in the epigenetic regulation of gene expression influencing developmental processes and cellular differentiation.
Specifications
Form
Liquid
General info
Function
DNA glycosylase that plays a key role in active DNA demethylation : specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine. Cannot remove 5-hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC. Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs : in the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine.
Sequence similarities
Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family.
Post-translational modifications
Sumoylation on Lys-330 by either SUMO1 or SUMO2 induces dissociation of the product DNA.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
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