Recombinant Human TDG Protein

Beta LifeScience SKU/CAT #: BLA-8865P

Recombinant Human TDG Protein

Beta LifeScience SKU/CAT #: BLA-8865P
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Product Overview

Host Species Human
Accession Q13569
Synonym C JUN leucine zipper interactive protein C-JUN leucine zipper interactive protein JZA-3 E130317C12Rik EC 3.2.2.29 G/T mismatch specific thymine DNA glycosylase G/T mismatch-specific thymine DNA glycosylase JZA 3 Jza1 T:G mismatch thymine glycosylase Tdg TDG_HUMAN Thymine DNA glycosylase Thymine-DNA glycosylase
Description Recombinant Human TDG Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
AA Sequence MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPA QEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITD TFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGH HYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGS KDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNL EFGLQPHKIPDTETLCYGMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLK GIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENP CSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCG TQEQEEESHA
Molecular Weight 71 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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.
Subcellular Location Nucleus.
Protein Families Uracil-DNA glycosylase (UDG) superfamily, TDG/mug family
Database References

Gene Functions References

  1. TET2- and TDG-mediated changes are required for the acquisition of distinct histone modifications in divergent terminal differentiation of myeloid cells. PMID: 28973458
  2. Results indicate how Thymine DNA glycosylase (TDG) employs an adaptable active site to excise a broad variety of nucleobases from DNA. PMID: 27805810
  3. 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
  4. findings indicate that sumoylation and SUMO binding are not essential for TDG-mediated excision and repair of 5-carboxylcytosine bases. PMID: 26917720
  5. 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
  6. A long TA repeat in the promoter region of IL28B was associated with spontaneous HCV clearance. PMID: 25735432
  7. 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
  8. Computational modeling study investigated the glycosidic bond cleavage reaction in human thymine DNA glycosylase PMID: 26320595
  9. levels of TET3 and TDG mRNAs were independent prognostic factors for early breast cancer patients who received anthracycline chemotherapy PMID: 26207381
  10. 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
  11. these results suggest that individuals harboring the G199S in Thymine DNA glycosylase variant may have increased risk for developing cancer. PMID: 25375110
  12. Data indicate that both thymine-DNA glycosylase (hTDG) and a second glycosylase, hOGG1, recognized structurally different 8-oxoguanine lesions. PMID: 25712093
  13. TDG, as a new coactivator, promotes beta-catenin/TCFs transactivation and functionally cooperates with CBP in canonical Wnt signaling. PMID: 24748645
  14. 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
  15. Results show TARID binds to the TCF21 promoter and recruits GADD45A and TDG to direct base excision repair for demethylation. PMID: 25087872
  16. 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
  17. these findings provide insights into the in vivo dynamics of TDG SUMOylation and further clarify the TDG-RNF4 interaction. PMID: 24727457
  18. Thymine DNA glycosylase is a positive regulator of Wnt signaling in colorectal cancer PMID: 24532795
  19. provide evidence for the existence of a functional ternary complex containing TDG, CBP and activated RARalpha PMID: 24394593
  20. 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
  21. 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
  22. 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
  23. Human thymine-DNA glycosylase is able to excise 8oxoA in 8oxoA*T pairs. PMID: 23209024
  24. A structural study of catalysis by the thymine DNA glycosylase catalytic domain. PMID: 22962365
  25. 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
  26. 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
  27. 5-carboxylcytosine is specifically recognized in the active site of thymine DNA glycosylase PMID: 22327402
  28. Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. PMID: 21862836
  29. DNMT3L exerts a major effect on the transcriptional regulation of a specific target gene, such as thymine DNA glycosylase PMID: 20428781
  30. 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
  31. the TDG-NCoA-3 interaction is important for broad range activation of steroid hormone nuclear receptors PMID: 19652917
  32. role in removing thymine produced by deamination of 5-methylcytosine and not removal of ethenocytosine PMID: 12493755
  33. Xeroderma pigmentosum group C protein interacts physically and functionally with this enzyme PMID: 12505994
  34. thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha PMID: 12874288
  35. Polymorphisms in thymine DNA Glycosylase is associated with lung Neoplasms PMID: 15225156
  36. unique range of each TDG activity corresponding to the three fractions indicates that human cells possibly express three distinct TDGs PMID: 15668625
  37. 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
  38. structure of the central region of human TDG conjugated to SUMO-1 at 2.1 A resolution PMID: 15959518
  39. Results describe the crystal structure of the central region of thymine-DNA glycosylase conjugated to SUMO-3. PMID: 16626738
  40. 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
  41. 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
  42. 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
  43. analysis of 5-halogenated uracils in human thymine DNA glycosylase PMID: 17602166
  44. Thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
  45. Expression of exogenous enzyme can functionally compensate for lower repair activities of damaged DNA in a myeloma cell line. PMID: 17965616
  46. A crystal structure of hTDG (catalytic domain, hTDG(cat)) in complex with abasic DNA, at 2.8 A resolution, is reported. PMID: 18587051
  47. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex PMID: 18805789
  48. These observations suggest that TDG modulates the biological function of p53 and other members of the p53 family as a transcriptional coactivator. PMID: 18951877
  49. 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
  50. 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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