Analytical Data
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Gene name
aTRX
- Application
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Alternative Names
aTRX；RAD54L；XH2；Transcriptional regulator ATRX
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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
P46100
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Expression Region
2311-2410aa
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AA Sequence
FNLGALSAMSNQQLEDLINQGREKVVEATNSVTAVRIQPLEDIISAVWKE NMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQMLISCVQRILM
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Molecular Weight
37 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
aTRX, a variant of thioredoxin, is a small redox-active protein that plays a crucial role in cellular processes, including regulating oxidative stress and facilitating protein folding. Research on aTRX has gained attention due to its potential therapeutic applications in various diseases, especially those related to oxidative damage and inflammation. The original thioredoxin proteins have been extensively studied for their role in redox biology, but aTRX stands out because of its unique structural features and enhanced stability. These properties make aTRX a promising candidate for recombinant protein engineering, where it can be utilized as a fusion partner to improve the solubility and stability of other proteins in biotechnological and pharmaceutical applications. Additionally, understanding the molecular mechanisms of aTRX's action may lead to innovative strategies for treating conditions such as cancer, neurodegenerative diseases, and cardiovascular disorders, where redox imbalances play a significant role. The ongoing exploration of aTRX and its recombinant forms may not only enhance our grasp of redox biology but also pave the way for the development of novel therapeutic interventions.
