Recombinant Thioredoxin / TRX protein (Active)
- Bioactive
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Recombinant Thioredoxin / TRX protein (Active) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
TRDX, TRX, TRX1, TXN, Thioredoxin, Trx, ATL-derived factor, Surface-associated sulphydryl protein, ADF, SASP
- FuncS
Supplier Data
Functional Studies - Recombinant Thioredoxin / TRX protein (Active) (AB286028)
Enzymatic activity of Trx : Trx reduction of Di-FITC-GSSG to FITC-GSH assay was performed in 26.5 mM potassium phosphate buffer, 1.5 mM EDTA, 1200 μU TrxR, and 610 μM NADPH. The reaction mix was incubated for 20 minutes at room temperature, which allows TrxR to reduce into Trx. Then Di-FITC-GSSG was added to the final concentration of 11.6 μM. FITC fluorescence was measured at 490/525 nm, which resulted in an activity curve with different amounts of Trx.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Thioredoxin / TRX protein (Active) (AB286028)
SDS-PAGE (4-20%) of Recombinant TRX : Recombinant protein loaded under reducing conditions and stained with Coomassie Blue. The protein shows a predicted MW of ~ 14.5 kDa
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Thioredoxin influences cellular redox homeostasis and plays direct roles in regulating cell growth and apoptosis. It participates as a major reductant in cells influencing transcription factors and enzymatic activities that depend on thiol-disulfide exchanges. Thioredoxin can interact with other components like thioredoxin reductase and NADPH to form the thioredoxin system a powerful antioxidant defense mechanism. Diseases typically arise from abnormal regulation of this system highlighting its influence on cellular survival and proliferation.
Pathways
Thioredoxin integrates into significant signaling and metabolic processes. It is an important player in the cellular response to oxidative stress and participates in signaling pathways such as the MAPK and apoptosis pathways. In these pathways thioredoxin reduces the oxidative stress transcription factor AP-1 influencing cell fate decisions. Its interaction with thioredoxin-interacting protein (TXNIP) further modulates cellular responses to oxidative environments.
Specifications
Form
Lyophilized
General info
Function
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed : 17182577, PubMed : 19032234, PubMed : 2176490). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity (PubMed : 16408020, PubMed : 17606900). Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (PubMed : 11118054, PubMed : 9108029).. ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).
Sequence similarities
Belongs to the thioredoxin family.
Post-translational modifications
In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins.. In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
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