Analytical Data
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Gene name
TREX2
- Application
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Alternative Names
3'-5' exonuclease TREX2
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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
Q9BQ50
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Expression Region
Met1~Ala236
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Molecular Weight
33kDa
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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
TREX2 (Three Prime Repair Exonuclease 2) is a nuclear enzyme that plays a crucial role in the maintenance of genomic stability by participating in DNA repair processes, particularly in the context of DNA double-strand breaks (DSBs). It functions primarily as a 3' to 5' exonuclease, which means it can degrade single-stranded DNA from the 3' end, thus facilitating the processing of DNA ends during repair. Dysregulation or malfunction of TREX2 has been implicated in various diseases, including cancer, where genomic instability is a hallmark. In cancer cells, improper DNA repair mechanisms can lead to the accumulation of mutations, contributing to tumorigenesis and progression. As a result, understanding the biochemical properties, regulation, and functional implications of TREX2 is of significant interest in the fields of molecular biology and cancer research. The study of TREX2 recombinant proteins allows researchers to investigate the enzyme's structural and functional characteristics in vitro, providing insight into its functional roles and potential consequences of its dysregulation. Advances in recombinant protein technology have facilitated the expression, purification, and characterization of TREX2, enabling detailed studies to elucidate its enzymatic activity, substrate specificity, and interaction with other repair proteins. Such research has the potential to uncover novel therapeutic targets for enhancing DNA repair in normal cells and mitigating the effects of genomic instability in cancer cells, thereby contributing to our understanding of cancer biology and the development of targeted therapies.
