Analytical Data
-
Gene name
TREX1
- Application
-
Alternative Names
TREX1；Three-prime repair exonuclease 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NSU2
-
Expression Region
1-304aa
-
AA Sequence
MQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPP PRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLA FLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALK ALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQW RPQALLRWVDAHARPFGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNT SPSLRESRGTKDLPPVKDPGALSREGLLAPLGLLAILTLAVATLYGLSLA TPGE
-
Molecular Weight
33.2 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
TREX1 (three prime repair exonuclease 1) is a crucial enzyme that plays a significant role in the cellular response to nucleic acid surveillance, particularly in the context of DNA metabolism and immune regulation. Mutations and dysfunction of TREX1 have been linked to various autoimmune diseases, including Aicardi-Goutières syndrome, systemic lupus erythematosus, and other inflammatory conditions. As a 3' to 5' exonuclease, TREX1 is responsible for degrading cytoplasmic nucleic acids that can arise from various sources, such as cellular DNA damage or viral infections. Its activity is essential for preventing the accumulation of these nucleic acids, which can otherwise trigger inappropriate immune responses and lead to autoimmunity. Research into the recombinant expression of TREX1 has gained traction as scientists seek to understand its structural and functional properties, elucidate its substrate specificity, and explore its regulatory mechanisms. Recombinant TREX1 proteins allow for detailed biochemical and biophysical studies that can enhance our understanding of the enzyme's role in nucleic acid homeostasis and immune modulation. By investigating TREX1 through recombinant approaches, researchers aim to delineate its potential therapeutic targets and develop strategies to modulate its activity in disease contexts, ultimately paving the way for novel treatments in autoimmune disorders and related pathologies.
