Recombinant Human TDG protein (denatured) is a Human Full Length protein, in the 1 to 410 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
M G S S H H H H H H S S G L V P R G S H M G S M E A E N A G S Y S L Q Q A Q A F Y T F P F Q Q L M A E A P N M A V V N E Q Q M P E E V P A P A P A Q E P V Q E A P K G R K R K P R T T E P K Q P V E P K K P V E S K K S G K S A K S K E K Q E K I T D T F K V K R K V D R F N G V S E A E L L T K T L P D I L T F N L D I V I I G I N P G L M A A Y K G H H Y P G P G N H F W K C L F M S G L S E V Q L N H M D D H T L P G K Y G I G F T N M V E R T T P G S K D L S S K E F R E G G R I L V Q K L Q K Y Q P R I A V F N G K C I Y E I F S K E V F G V K V K N L E F G L Q P H K I P D T E T L C Y G M P S S S A R C A Q F P R A Q D K V H Y Y I K L K D L R D Q L K G I E R N M D V Q E V Q Y T F D L Q L A Q E D A K K M A V K E E K Y D P G Y E A A Y G G A Y G E N P C S S E P C G F S S N G L I E S V E L R G E S A F S G I P N G Q W M T Q S F T D Q I P S F S N H C G T Q E Q E E E S H A
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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.
G/T mismatch-specific thymine DNA glycosylase, Thymine-DNA glycosylase, hTDG, TDG
Recombinant Human TDG protein (denatured) is a Human Full Length protein, in the 1 to 410 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.58% Sodium chloride, 0.32% Tris HCl
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.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family.
Sumoylation on Lys-330 by either SUMO1 or SUMO2 induces dissociation of the product DNA.
Previously labelled as Thymine DNA glycosylase.
TDG also known as thymine DNA glycosylase is an enzyme that plays a critical role in DNA repair. It has a molecular mass of approximately 45 kDa. TDG removes thymine and other modified bases from DNA that are paired with guanine which initiates the process of base excision repair. This mechanism is essential for maintaining genomic integrity. TDG is expressed in various tissues including the brain liver and testes reflecting its importance in diverse physiological contexts.
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.
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.
TDG's function has implications for cancer and neurodegenerative diseases. Altered TDG activity can lead to genomic instability contributing to the progression of cancer by allowing the accumulation of mutations. Furthermore disruptions in DNA repair mechanisms including those involving TDG have been linked to neurodegenerative diseases such as Alzheimer's disease. In cancer proteins like MSH6 in the mismatch repair pathway might interact with TDG when aberrant repair occurs. In neurodegenerative disorders changes in TDG activity might interact with proteins involved in neuronal function and stability exacerbating disease mechanisms.
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15% SDS-PAGE analysis of 3 μg ab134525.
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