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Human TDG Protein expressed in Escherichia coli (E. coli) - ABIN1098673
Um, Harbers, Benecke, Pierrat, Losson, Chambon: Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase. in The Journal of biological chemistry 1998
Show all 2 references for ABIN1098673
miR (show MYLIP Proteins)-29b targets LPL (show LPL Proteins) and TDG genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
CRL4(Cdt2) targets thymine DNA glycosylase (TDG), a base excision repair enzyme that is involved in DNA demethylation
TDG gene knockdown could inhibit the differentiation of pig pre-adipocytes and affect the DNA methylation (show HELLS Proteins) levels of certain transcription factors.
The DNA demethylation marks are dynamically regulated in both in vivo and in vitro aging conditions, which are associated with Tet3 over-expression and Tdg repression.
TDG, as a new coactivator, promotes beta-catenin (show CTNNB1 Proteins)/TCFs transactivation and functionally cooperates with CBP (show CREBBP Proteins) in canonical Wnt (show WNT2 Proteins) signaling.
Embryonic lethality in Tdg (-/-) embryos is due, in part, to the reduction of noradrenaline levels.
data suggest that oxidation of 5-methylcytosine by Tet proteins followed by TDG-mediated base excision of 5-carboxylcytosine constitutes a pathway for active DNA demethylation
Results demonstrate that TDG is required for normal mammalian development and the establishment of proper promoter/enhancer DNA methylation (show HELLS Proteins) patterns that are conducive to transcription during embryogenesis
TDG-dependent DNA repair has evolved to provide epigenetic stability in lineage committed cells
Association of CBP/p300 (show CREBBP Proteins) acetylase and TDG links DNA repair and transcription.
binds SUM0-1; TDGb was also shown to interact with the promyelocytic leukemia protein (PML (show PML Proteins)) in vitro as well as to colocalize with this protein to nuclear bodies in transfected cells
TDG sumoylation promotes intramolecular interactions with amino- and carboxy-terminal SUMO-1 (show SUMO1 Proteins) binding motifs that dramatically alter the biochemical properties and subcellular localization of TDG
Data report the characterization of interactions between Dnmt3b (show DNMT3B Proteins) and both thymine-DNA glycosylase (Tdg) and methyl-CpG binding domain protein 4 (show MBD4 Proteins).
Results indicate the presence of base excision repair -dependent and base excision repair-independent functions of TDG, which are involved in regulation of cellular DNA damage responses and gene expression patterns.
findings indicate that sumoylation and SUMO binding are not essential for TDG-mediated excision and repair of 5-carboxylcytosine bases.
Data show that Ras protein regulates inhibitor of growth protein 4 (ING4 (show ING4 Proteins))-thymine-DNA glycosylase (TDG)-Fas (show FAS Proteins) protein axis to promote apoptosis resistance in pancreatic cancer.
A long TA repeat in the promoter region of IL28B (show IL28B Proteins) was associated with spontaneous HCV clearance.
NEIL1 (show NEIL1 Proteins) and NEIL2 (show NEIL2 Proteins) cooperate with TDG during base excision: TDG occupies the abasic site and is displaced by NEILs, which further process the baseless sugar, thereby stimulating TDG-substrate turnover.
Computational modeling study investigated the glycosidic bond cleavage reaction in human thymine DNA glycosylase
levels of TET3 and TDG mRNAs were independent prognostic factors for early breast cancer patients who received anthracycline chemotherapy
TDG releases the excised base from its tight product complex with abasic DNA, contrary to previous reports. Moreover, DNA-free TDG exhibits no significant binding to free nucleobases (uracil, thymine, 5-hydroxymethyluracil)
these results suggest that individuals harboring the G199S in Thymine DNA glycosylase variant may have increased risk for developing cancer.
Data indicate that both thymine-DNA glycosylase (hTDG) and a second glycosylase, hOGG1, recognized structurally different 8-oxoguanine lesions.
The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings. TDG can also remove uracil and 5-bromouracil from mispairings with guanine. This enzyme plays a central role in cellular defense against genetic mutation caused by the spontaneous deamination of 5-methylcytosine and cytosine. This gene may have a pseudogene in the p arm of chromosome 12.
G/T mismatch-specific thymine DNA glycosylase
, G/T mismatch DNA glycosylase
, G/t mismatch-specific thymine DNA glycosylase
, thymine-DNA glycosylase
, G/T mismatch-specific thymine DNA glycosylase-like
, g/T mismatch-specific thymine DNA glycosylase-like
, C-JUN leucine zipper interactive protein JZA-3