Analytical Data
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Gene name
Thioredoxin/TRX
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简介
Thioredoxin/TRX proteins participate in multiple redox reactions, utilizing their reactive dithiol centers for reversible oxidation and disulfide bond formation.It catalyzes important dithiol-disulfide exchange and plays a key role in S-nitrosylation of cysteine residues in response to intracellular nitric oxide.Thioredoxin/TRX Protein, Mouse (N-His) is the recombinant mouse-derived Thioredoxin/TRX protein, expressed by E.coli , with N-6*His labeled tag.
- Application
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Alternative Names
Thioredoxin; TXN; Trx; ADF; TRX1; SASP
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Species
Mouse
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P10639
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Expression Region
M1-A105
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Protein Length
Full Length
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Molecular Weight
15 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 (TRX) is a small, evolutionary-conserved redox protein that plays a crucial role in various biological processes, including antioxidant defense, redox regulation, and protein folding. It contains a well-characterized active site with a dithiol-disulfide mechanism, enabling it to facilitate the reduction of disulfide bonds in substrates. Research on TRX has intensified due to its involvement in critical cellular functions and its implications in various diseases, including cancer, diabetes, and neurodegenerative disorders. Recombinant TRX proteins have been produced for biochemical and biophysical studies, offering insights into their structure-function relationships and mechanisms of action. Furthermore, TRX has emerged as a potential therapeutic target, as its redox activity can impact cellular signaling pathways and promote cell survival under oxidative stress. Advances in recombinant DNA technology have enabled the generation of engineered TRX variants with altered properties for specific applications, such as drug delivery, enzyme stabilization, and the enhancement of biocatalytic processes. Understanding the functionalities and interactions of TRX at a molecular level paves the way for innovative strategies in biomedical research and therapeutic development.
