Recombinant Human G/T Mismatch-Specific Thymine Dna Glycosylase (TDG) Protein (His)

Name: Recombinant Human G/T Mismatch-Specific Thymine Dna Glycosylase (TDG) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07459P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human G/T Mismatch-Specific Thymine Dna Glycosylase (TDG) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13569
Target Symbol	TDG
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPAQEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA
Expression Range	1-410aa
Protein Length	Full Length
Mol. Weight	52.1 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 11700 OMIM: 601423 KEGG: hsa:6996 STRING: 9606.ENSP00000376611 UniGene: 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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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.

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