Analytical Data
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Gene name
trxA
- Application
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Alternative Names
trxA；Thioredoxin
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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
P41252
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Expression Region
1172-1262aa
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AA Sequence
QYINLQLLNAKPQECLMGTVGTLLLENPLGQNGLTHQGLLYEAAKVFGLR SRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTADF
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Molecular Weight
36 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
The trxA gene encodes thioredoxin, a key protein involved in various cellular processes, including redox regulation, antioxidant defense, and protein folding. Research on recombinant trxA protein is significant due to its potential applications in biotechnology and medicine. Thioredoxin plays a crucial role in maintaining the redox balance within cells, thus contributing to cellular homeostasis and protecting against oxidative stress. In microbial systems, recombinant trxA can be exploited for improving protein solubility and stability, facilitating the production of other recombinant proteins. Moreover, studies have demonstrated that thioredoxin can enhance the activity of certain enzymes, which has implications for metabolic engineering and biocatalysis. Additionally, the potential use of trxA in therapeutic applications, such as cancer treatment and neuroprotection, underlines its biological importance. Investigating the production, purification, and functional characteristics of recombinant trxA can lead to valuable insights into its mechanistic roles in vivo and its utility in industrial applications. Overall, the study of trxA and its recombinant forms holds promise for advancing our understanding of cellular mechanisms and developing innovative biotechnological solutions.
