Recombinant human Thioredoxin / TRX protein (His tag N-Terminus)
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Recombinant human Thioredoxin / TRX protein (His tag N-Terminus) 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
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
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
Liquid
Additional notes
ab95319 is purified using conventional chromatography techniques.
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
Product promise
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