Analytical Data
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Gene name
TXN2
- Application
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Alternative Names
TXN2；KIAA1652；Thioredoxin reductase 2. mitochondrial
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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
Q99757
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Expression Region
1-166aa
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AA Sequence
TTFNIQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAMKNGDVVDKFVGIKDEDQLEAFLKKLIG
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Molecular Weight
38.9kDa
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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
TXN2, or Thioredoxin 2, is a critical protein implicated in various cellular processes, including redox regulation, apoptosis, and the response to oxidative stress. It belongs to the thioredoxin family, which is characterized by its ability to facilitate the reduction of disulfide bonds in proteins, thereby playing a vital role in maintaining cellular redox homeostasis. Research on TXN2 has gained significant attention due to its potential implications in numerous pathophysiological conditions, including cancer, cardiovascular diseases, and neurodegenerative disorders. Understanding the structural and functional aspects of TXN2 through recombinant protein studies is essential for elucidating its biological roles and mechanisms of action. Recombinant TXN2 allows for detailed investigations into its enzymatic activities, interaction with other cellular components, and involvement in signaling pathways. Additionally, TXN2's role in mitigating oxidative damage and regulating apoptosis underscores its potential as a therapeutic target. Overall, the study of TXN2 recombinant protein contributes to the broader understanding of redox biology and offers insights into novel therapeutic strategies for conditions associated with oxidative stress and dysfunctional redox signaling.
