Analytical Data
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Gene name
Thioredoxin-1/TRXA
- Application
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Alternative Names
trxA; fipA; tsnC; b3781; JW5856; Thioredoxin 1; Trx-1
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Species
Escherichia coli
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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
P0AA25
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Expression Region
2-109aa
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Molecular Weight
15.7 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
Thioredoxin-1 (TRX) is a small redox-active protein that plays a crucial role in cellular processes by maintaining the redox balance, facilitating protein folding, and regulating cell signaling pathways. Its importance is underscored by its involvement in various biological functions, including apoptosis, immune response, and oxidative stress management. Recombinant TRX, or TRXA, is engineered for experimental and therapeutic applications, allowing researchers to explore its mechanisms in greater detail. The recombination process enhances TRX’s availability and enables controlled studies of its interactions with target proteins, providing insights into its dual functions as a chaperone and antioxidant. Furthermore, given its potential as a therapeutic agent, understanding TRXA's structure and function is critical in the development of novel treatments for diseases characterized by oxidative stress, such as cancer and neurodegenerative disorders. The production of recombinant TRX also opens avenues for biotechnological applications, including the design of novel redox-based biosensors and drug delivery systems, thereby positioning TRX as a significant protein in both basic and applied research.
