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

Beta LifeScience SKU/CAT #: BLT-03002P
SDS-PAGE analysis of Human TDG (G/T Mismatch-Specific Thymine Dna Glycosylase) - Recombinant Protein, CAT
SDS-PAGE analysis of Human TDG (G/T Mismatch-Specific Thymine Dna Glycosylase) - Recombinant Protein, CAT# BLT-03002P, showing >90% purity under 15% SDS-PAGE (Reduced)

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

Beta LifeScience SKU/CAT #: BLT-03002P
Regular price $595.00 Sale price $445.00Save $150
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Pack Size Price (USD)
500 µg $1,030 (Fall Promotion)
1 mg $1,870 (Fall Promotion)

For direct online orders, quantity pricing will be displayed in cart when you add 5x100ug or 10x100ug


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Product Overview

Product Name Recombinant Human Thymine DNA Glycosylase (TDG) Protein
Product Overview This recombinant human Thymine DNA Glycosylase (TDG) protein includes amino acids 1-410aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id Q13569
Recommended Name G/T mismatch-specific thymine DNA glycosylase
Gene Name TDG
Synonyms Thymine-DNA glycosylase, G/T mismatch-specific thymine DNA glycosylase,
Species Human
Predicted Molecular Mass 70 kDa
Expression System E.coli
Expression Range 1-410aa
Tag N-6His+SUMO
Purity >90%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 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.
Reconstitution Instruction 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%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Epigenetics And Nuclear Signaling
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 Family Uracil-DNA glycosylase (UDG) superfamily, TDG/mug family

FAQs

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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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