Analytical Data
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Gene name
TDG
- Application
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Alternative Names
(Thymine-DNA glycosylase)(hTDG)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13569
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Expression Region
1-410aa
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Molecular Weight
52.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of TDG (thymine DNA glycosylase) recombinant proteins has gained significant attention due to their crucial role in maintaining genomic stability and their implications in various biological processes, including DNA repair and epigenetic regulation. TDG is a DNA glycosylase that specifically recognizes and excises mismatched thymine bases in DNA, which can result from oxidative damage or deamination events. Dysfunction in TDG activity is associated with various diseases, including cancer, emphasizing the need for a deeper understanding of its mechanisms. Moreover, TDG is linked to the regulation of gene expression through its interactions with 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC), which are essential for epigenetic modifications. Research has focused on producing recombinant forms of TDG to investigate its structure-function relationships, enzyme kinetics, and interactions with other molecular components. These recombinant proteins enable the exploration of TDG's role in DNA repair pathways and its potential as a therapeutic target. Furthermore, advancements in recombinant protein technology have facilitated the purification and characterization of TDG, allowing for greater insights into its biological functions and its potential applications in biotechnology and medicine. As such, the ongoing research into TDG recombinant proteins is not only pivotal for understanding fundamental biological processes but also holds promise for developing novel therapeutic strategies in treating diseases linked to improper DNA repair mechanisms.
