Product Description
Size: 100µg / 500µg
Recombinant human Thioredoxin / TRX protein (Active) is a Human Full Length protein, in the 1 to 105 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS, WB.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:SDS-PAGE, FuncS, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity is >150 A650/cm/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.,
Accession:P10599,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.4Constituents: PBS
Product details:
MW confirmed by MALDI-TOF.
Concentration determined by BCA assay.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
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.
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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Collaboration
Tony Tang
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