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% purity and suitable for SDS-PAGE, FuncS, WB.
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- Clinical cancer research : an official journal of 25:7162-71742019Bioactivation of Napabucasin Triggers Reactive Oxygen Species-Mediated Cancer Cell Death.Applications:Unspecified applicationReactive species:Unspecified reactive speciesFieke E M Froeling et. al.PubMed 31527169
- Nature communications 10:40732019Spatial oxidation of L-plastin downmodulates actin-based functions of tumor cells.Applications:Unspecified applicationReactive species:Unspecified reactive speciesEmre Balta et. al.PubMed 31501427
- Journal of applied physiology (Bethesda, Md. : 198 127:858-8662019Characterization of extracellular redox enzyme concentrations in response to exercise in humans.Applications:Unspecified applicationReactive species:Unspecified reactive speciesAlex J Wadley et. al.PubMed 31246554
- Cell chemical biology 26:449-461.e82019Selective Disruption of Mitochondrial Thiol Redox State in Cells and In Vivo.Applications:Unspecified applicationReactive species:Unspecified reactive speciesLee M Booty et. al.PubMed 30713096
- Chemistry Central journal 7:1502013Healthy ageing and depletion of intracellular glutathione influences T cell membrane thioredoxin-1 levels and cytokine secretion.Applications:Unspecified applicationReactive species:Unspecified reactive speciesRita Barreto Duarte Carilho Torrao et. al.PubMed 24007191
- PloS one 6:e219262011Orally active multi-functional antioxidants are neuroprotective in a rat model of light-induced retinal damage.
Key facts
- Purity
- >95% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, FuncS, WB
- Biologically active
- Yes
Amino acid sequence
M V K Q I E S K T A F Q E A L D A A G D K L V V V D F S A T W C G P C K M I K P F F H S L S E K Y S N V I F L E V D V D D C Q D V A S E C E V K C M P T F Q F F K K G Q K V G E F S G A N K E K L E A T I N E L V
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes ab51064 can be used as a WB positive control in conjunction with Anti-Thioredoxin / TRX antibody ab26320. |
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Target data
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).
Alternative names
TRDX, TRX, TRX1, TXN, Thioredoxin, Trx, ATL-derived factor, Surface-associated sulphydryl protein, ADF, SASP
Recommended products
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% purity and suitable for SDS-PAGE, FuncS, WB.
Key facts
- Purity
- >95% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, FuncS, WB
- 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
- P10599-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7.4
Constituents: PBS
Sequence info
Amino acid sequence
- M V K Q I E S K T A F Q E A L D A A G D K L V V V D F S A T W C G P C K M I K P F F H S L S E K Y S N V I F L E V D V D D C Q D V A S E C E V K C M P T F Q F F K K G Q K V G E F S G A N K E K L E A T I N E L V
- Accession
- P10599
- Protein length
- Full Length
- Predicted molecular weight
- 11.7 kDa
- Amino acids
- 1 to 105
- Nature
- Recombinant
Specifications
- Form
- Liquid
- Additional notes
Recombinant human Thioredoxin / TRX was overexpressed in *E. coli* and purified by 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).
- 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.
- Subcellular localisation
- Nucleus
Storage
- 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
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
MW confirmed by MALDI-TOF.
Concentration determined by BCA assay.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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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2 product images
Western blot - Recombinant human Thioredoxin / TRX protein (Active) (ab51064)
All lanes: Western blot - Anti-Thioredoxin / TRX antibody (Anti-Thioredoxin / TRX antibody ab26320) at 1 µg/mL
All lanes: Western blot - Recombinant human Thioredoxin / TRX protein (Active) (ab51064) at 0.01 µg
SecondaryAll lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (Goat Anti-Rabbit IgG H&L (HRP) preadsorbed ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 12 kDa
Exposure time: 30s
SDS-PAGE - Recombinant human Thioredoxin / TRX protein (Active) (ab51064)
3 ug of reduced ab51064, on 15% SDS-PAGE, stained with Coomassie Blue.
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