Analytical Data
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Gene name
TXN2
- Application
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Alternative Names
MT-TRX; TRX2; MTRX
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Species
Bovine
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q95108
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Expression Region
Thr60~Gly166
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Molecular Weight
16kDa
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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 (Thioredoxin 2) is a crucial member of the thioredoxin family, primarily localized in mitochondria, playing a vital role in cellular redox regulation and mitochondrial function. It is involved in protecting cells from oxidative stress by facilitating the reduction of disulfide bonds in proteins, thereby maintaining protein stability and functionality. Research on recombinant TXN2 protein has gained significance due to its potential implications in various pathophysiological conditions, including neurodegenerative diseases, cancer, and cardiovascular diseases, where oxidative stress is a contributing factor. The ability to produce TXN2 in a recombinant form allows for detailed studies on its biochemical properties, interaction with other cellular molecules, and the elucidation of its role in cell signaling pathways. Furthermore, recombinant TXN2 is being explored for its therapeutic potential, as enhancing its activity could mitigate oxidative damage and promote cellular health. Consequently, understanding TXN2's structure-function relationship and its involvement in mitochondrial dynamics is of paramount importance, paving the way for innovative strategies in disease intervention and treatment.
