Analytical Data
-
Gene name
Thioredoxin/TXN
- Application
-
Alternative Names
rEcoThioredoxin/TXN, His; Trx; ADF; TRX1
-
Species
E.coli
-
Source
E. coli
-
Tag
C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
M26133
-
Expression Region
M1-A109
-
Protein Length
Full Length
-
Molecular Weight
13 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Thioredoxin (TXN) is a small redox protein that plays a crucial role in maintaining the cellular redox balance and regulating various physiological processes, including cell growth, differentiation, and apoptosis. Its function is primarily mediated through the presence of a conserved active site cysteine pair that can undergo reversible oxidation and reduction, enabling TXN to act as an electron donor for other proteins and promoting the reduction of disulfide bonds. Given its significant role in cellular metabolism and stress response, TXN has garnered extensive research interest, especially in the fields of cancer therapy, neurobiology, and redox biology. The development of recombinant thioredoxin proteins allows for detailed studies of their structure-function relationships and interactions with other biomolecules. Additionally, TXN has potential as a therapeutic target, as its overexpression is often associated with tumor progression and resistance to chemotherapy. By utilizing recombinant DNA technology, researchers can produce TXN in sufficient quantities for biochemical assays and therapeutic applications, providing insights into its role in various diseases and its potential use as a biomarker or drug target. The advancements in TXN research highlight its importance in understanding the intricate balance of redox states in cells and the implications this balance has for health and disease. Overall, the study of recombinant thioredoxin proteins is a promising avenue for both fundamental biological research and the development of novel therapeutic strategies.
