Recombinant human Thioredoxin / TRX protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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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).
TRDX, TRX, TRX1, TXN, Thioredoxin, Trx, ATL-derived factor, Surface-associated sulphydryl protein, ADF, SASP
Recombinant human Thioredoxin / TRX protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
pH: 7.4
Constituents: PBS
ab95319 is purified using conventional chromatography techniques.
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).
Belongs to the thioredoxin family.
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.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Thioredoxin (TRX) also known as TXN or Trx is a small redox protein with a molecular mass of approximately 12 kDa. It acts as an oxidoreductase enzyme facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxin is ubiquitously expressed across various tissues indicating its function in a broad range of cellular activities. The protein comprises an active site with a conserved Cys-Gly-Pro-Cys sequence critical for its reducing activity.
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.
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.
Altered thioredoxin activity associates with cancer and neurodegenerative diseases. Its overexpression links to tumor progression where it promotes survival and resistance to apoptosis. Additionally in the context of neurodegenerative disorders thioredoxin’s interaction with amyloid-beta peptides implicates it in Alzheimer’s disease by mitigating oxidative stress damage. Through these conditions its role as a protector against oxidative stress remains pivotal.
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