Name: Recombinant Human G/T mismatch-specific thymine DNA glycosylase (TDG)
Brand: CUSABIO
SKU: CSB-EP623816HU

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

TDG

Uniprot No.

Q13569

Research Area

Epigenetics and Nuclear Signaling

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

1-410aa

Target Protein Sequence

MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPAQEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

52.1 kDa

Protein Length

Full Length

Tag Info

N-terminal 10xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Customer Reviews and Q&A

■ Customer Reviews

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■ Q&A

Is this product (CSB-EP623816HU ) a denatured protein? or Is it supposed to have its normal structure?

CSB-EP623816HU is expressed in inclusion bodies, it is refolded after the expression and we can ensure that the final products that we provide is soluble. However, we haven't tested the structure of CSB-EP623816HU.
We recommend the following partial protein CSB-EP623816HU1(111-308aa; partial), which is a supernatant protein.

Target Background

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.

Gene References into Functions

TET2- and TDG-mediated changes are required for the acquisition of distinct histone modifications in divergent terminal differentiation of myeloid cells. PMID: 28973458
Results indicate how Thymine DNA glycosylase (TDG) employs an adaptable active site to excise a broad variety of nucleobases from DNA. PMID: 27805810
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. PMID: 28318075
findings indicate that sumoylation and SUMO binding are not essential for TDG-mediated excision and repair of 5-carboxylcytosine bases. PMID: 26917720
Data show that Ras protein regulates inhibitor of growth protein 4 (ING4)-thymine-DNA glycosylase (TDG)-Fas protein axis to promote apoptosis resistance in pancreatic cancer. PMID: 26544625
A long TA repeat in the promoter region of IL28B was associated with spontaneous HCV clearance. PMID: 25735432
NEIL1 and NEIL2 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. PMID: 26751644
Computational modeling study investigated the glycosidic bond cleavage reaction in human thymine DNA glycosylase PMID: 26320595
levels of TET3 and TDG mRNAs were independent prognostic factors for early breast cancer patients who received anthracycline chemotherapy PMID: 26207381
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) PMID: 26358812
these results suggest that individuals harboring the G199S in Thymine DNA glycosylase variant may have increased risk for developing cancer. PMID: 25375110
Data indicate that both thymine-DNA glycosylase (hTDG) and a second glycosylase, hOGG1, recognized structurally different 8-oxoguanine lesions. PMID: 25712093
TDG, as a new coactivator, promotes beta-catenin/TCFs transactivation and functionally cooperates with CBP in canonical Wnt signaling. PMID: 24748645
CRL4(Cdt2)-dependent degradation of TDG occurs in S phase because of the requirement for TDG to interact with chromatin-loaded PCNA, and this degradation is important for preventing toxicity from excess TDG. PMID: 24962565
Results show TARID binds to the TCF21 promoter and recruits GADD45A and TDG to direct base excision repair for demethylation. PMID: 25087872
Whereas sumoylation substantially weakens TDG binding to DNA, TDG approximately SUMO-1 still binds relatively tightly to AP-DNA (Kd approximately 50 nM). PMID: 24753249
these findings provide insights into the in vivo dynamics of TDG SUMOylation and further clarify the TDG-RNF4 interaction. PMID: 24727457
Thymine DNA glycosylase is a positive regulator of Wnt signaling in colorectal cancer PMID: 24532795
provide evidence for the existence of a functional ternary complex containing TDG, CBP and activated RARalpha PMID: 24394593
SIRT1 affects DNA repair through binding to thymine DNA glycosylase (TDG), stimulating TDG glycosylase activity, maintaining TDG in a hypoacetylated state, and regulating TDG expression PMID: 23952905
Results imply that 5-carboxylcytosine (5caC) can adopt alternative conformations (either N157-interacting or N230-interacting) in the thymine DNA glycosylase active site to interact with either of the two asparagine side chain for 5caC excision. PMID: 23680598
TDG 3'untranslated region (UTR) contains two miR-29 binding sites; the miR-29 mimic decreases TDG mRNA by 40%, while miR-29 inhibitor increases TDG mRNA by 43.7% in human vascular smooth muscle cell cultures. PMID: 23820384
Human thymine-DNA glycosylase is able to excise 8oxoA in 8oxoA*T pairs. PMID: 23209024
A structural study of catalysis by the thymine DNA glycosylase catalytic domain. PMID: 22962365
genetic variants in TDG, important not only in base excision repair but also in regulating the epigenome and gene expression, which may contribute to the non-melanoma skin cancer associated increase in overall cancer risk. PMID: 22581838
We solved a crystal structure of TDG (catalytic domain) bound to a substrate analog and characterized active-site residues by mutagenesis, kinetics, and molecular dynamics simulations. PMID: 22573813
5-carboxylcytosine is specifically recognized in the active site of thymine DNA glycosylase PMID: 22327402
Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. PMID: 21862836
DNMT3L exerts a major effect on the transcriptional regulation of a specific target gene, such as thymine DNA glycosylase PMID: 20428781
Studies lead to the characterization of a small structural domain in the TDG N-terminal region preceding the catalytic core and coinciding with the region of functional regulation of TDG's activities. PMID: 18512959
the TDG-NCoA-3 interaction is important for broad range activation of steroid hormone nuclear receptors PMID: 19652917
role in removing thymine produced by deamination of 5-methylcytosine and not removal of ethenocytosine PMID: 12493755
Xeroderma pigmentosum group C protein interacts physically and functionally with this enzyme PMID: 12505994
thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha PMID: 12874288
Polymorphisms in thymine DNA Glycosylase is associated with lung Neoplasms PMID: 15225156
unique range of each TDG activity corresponding to the three fractions indicates that human cells possibly express three distinct TDGs PMID: 15668625
Upon DNA interaction, TDG undergoes a dramatic conformational change, which involves its flexible N-terminal domain and accounts for its nonspecific DNA binding ability during base excision repair. PMID: 15823533
structure of the central region of human TDG conjugated to SUMO-1 at 2.1 A resolution PMID: 15959518
Results describe the crystal structure of the central region of thymine-DNA glycosylase conjugated to SUMO-3. PMID: 16626738
A novel missense variant A196G was found in familial colorectal cancer DNA suggesting a limited role for this gene in the devlopment of CRC. PMID: 17029639
TDG sumoylation promotes intramolecular interactions with amino- and carboxy-terminal SUMO-1 binding motifs that dramatically alter the biochemical properties and subcellular localization of TDG PMID: 17060459
The ability of human thymine-DNA glycosylase (TDG) to excise 8-(hydroxymethyl)-3,N(4)-ethenocytosine (8-hm-varepsilonC) and 3,N(4)-ethanocytosine (EC) was investigated and compared with varepsilonC, a known substrate for TDG. PMID: 17270163
analysis of 5-halogenated uracils in human thymine DNA glycosylase PMID: 17602166
Thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
Expression of exogenous enzyme can functionally compensate for lower repair activities of damaged DNA in a myeloma cell line. PMID: 17965616
A crystal structure of hTDG (catalytic domain, hTDG(cat)) in complex with abasic DNA, at 2.8 A resolution, is reported. PMID: 18587051
Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex PMID: 18805789
These observations suggest that TDG modulates the biological function of p53 and other members of the p53 family as a transcriptional coactivator. PMID: 18951877
There was a 1.198-fold increased micronucleus frequency for individuals carrying TDG 199Gly/Ser + Ser/Ser genotypes compared with those carrying Gly/Gly genotype (P < 0.05) for exposure to vinyl chloride. PMID: 19369898
excision of DNA-incorporated 5-FU by TDG generates persistent DNA strand breaks, delays S-phase progression, and activates DNA damage signaling PMID: 19402749

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Subcellular Location

Nucleus.

Protein Families

Uracil-DNA glycosylase (UDG) superfamily, TDG/mug family

Database Links

HGNC: 11700

OMIM: 601423

KEGG: hsa:6996

STRING: 9606.ENSP00000376611

UniGene: Hs.584809

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