Recombinant human Thioredoxin / TRX protein (Active) (Tag Free)
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(6 Publications)
Recombinant human Thioredoxin / TRX protein (Active) (Tag Free) 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.
View Alternative Names
TRDX, TRX, TRX1, TXN, Thioredoxin, Trx, ATL-derived factor, Surface-associated sulphydryl protein, ADF, SASP
- WB
Unknown
Western blot - Recombinant human Thioredoxin / TRX protein (Active) (Tag Free) (AB51064)
All lanes:
Western blot - Anti-Thioredoxin / TRX antibody (<a href='/en-us/products/primary-antibodies/thioredoxin-trx-antibody-ab26320'>ab26320</a>) at 1 µg/mL
All lanes:
Western blot - Recombinant human Thioredoxin / TRX protein (Active) (Tag Free) (ab51064) at 0.01 µg
Secondary
All lanes:
Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution
Predicted band size: 12 kDa
true
Exposure time: 30s
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Thioredoxin / TRX protein (Active) (AB51064)
3 ug of reduced ab51064, on 15% SDS-PAGE, stained with Coomassie Blue.
Reactivity data
Product details
MW confirmed by MALDI-TOF.
Concentration determined by BCA assay.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
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
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).. 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
Publications (6)
Recent publications for all applications. Explore the full list and refine your search
Clinical cancer research : an official journal of 25:7162-7174 PubMed31527169
2019
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Unspecified reactive species
Nature communications 10:4073 PubMed31501427
2019
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Journal of applied physiology (Bethesda, Md. : 198 127:858-866 PubMed31246554
2019
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Unspecified reactive species
Cell chemical biology 26:449-461.e8 PubMed30713096
2019
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Chemistry Central journal 7:150 PubMed24007191
2013
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PloS one 6:e21926 PubMed21779355
2011
Applications
WB
Species
Unspecified reactive species
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