Analytical Data
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Gene name
TDG
- Application
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Alternative Names
TDG；G/T mismatch-specific thymine DNA glycosylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPA QEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITD TFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGH HYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGS KDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNL EFGLQPHKIPDTETLCYGMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLK GIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENP CSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCG TQEQEEESHA
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Molecular Weight
71 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
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Protein Description
The study of TDG (Thymine-DNA Glycosylase) recombinant protein has garnered significant attention in the field of molecular biology and genetics due to its crucial role in DNA repair mechanisms. TDG is a DNA glycosylase that specifically recognizes and excises non-canonical bases such as thymine mismatched with guanine, which can arise due to deamination processes or oxidative damage. This function is vital for maintaining genomic stability and preventing mutations that can lead to various diseases, including cancer. Research into TDG recombinant protein focuses on understanding its structural properties, enzymatic activity, and interactions with other repair proteins. The development of TDG as a recombinant protein allows scientists to produce it in vitro for detailed biochemical studies, enabling the investigation of its role in repair pathways and elucidating the underlying mechanisms of DNA damage response. Moreover, the potential therapeutic implications of TDG in gene editing and cancer treatment strategies make it an attractive target for further research. Understanding TDG's function could pave the way for innovative approaches in combating genetic disorders and improving genome integrity.
