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Human Monoclonal TXN2 Primary Antibody for IP - ABIN532604
Arnér, Holmgren: Physiological functions of thioredoxin and thioredoxin reductase. in European journal of biochemistry / FEBS 2000
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Human Monoclonal TXN2 Primary Antibody for IP - ABIN532603
Nordberg, Arnér: Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. in Free radical biology & medicine 2001
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Human Polyclonal TXN2 Primary Antibody for ELISA, WB - ABIN543430
Chen, Cai, Murphy, Jones: Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. in The Journal of biological chemistry 2002
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Human Polyclonal TXN2 Primary Antibody for ICC, IF - ABIN4359198
Dammeyer, Arnér: Human Protein Atlas of redox systems - what can be learnt? in Biochimica et biophysica acta 2010
Overexpression of mitochondrial Trx2 attenuates the intracellular ROS accumulation and ATP production. Most interestingly, mitochondrial Trx2 may be involved in the cardiac hypertrophy signaling of diabetes.
Prx3 and Trx2 comprise an adaptive system to sense changes in atmospheric oxygen tension and influence cellular injury responses through both detoxification of mitochondrial oxidants and regulation of mitochondrial redox-dependent signaling
Trx2 overexpression failed to attenuate hypoxia-induced human pulmonary arterial smooth muscle cells proliferation in vitro or hypoxia-induced Pulmonary hypertension in vivo.
study demonstrated that miR-27a and -b, which are widely expressed in host cells, suppress SNAP25 and TXN2 expression through posttranscriptional gene silencing.
No evidence that SNPs in TRX2 have effects, but the rs4485648 polymorphism of the TrxR2 gene might exert an independent effect on the development of Diabetic retinopathy.
Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the Replication of Classical Swine Fever Virus by promoting the nuclear translocation of the p65 subunit of NF-kappaB.
The Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.
CERKL interacts with TRX2 and plays a novel key role in the regulation of the TRX2 antioxidant pathway.
TGF-beta-mediated expression of the epithelial-mesenchymal transition marker fibronectin was inhibited not only by chemicals that interfere with reactive oxygen species signaling but also by exogenously expressed mitochondrial thioredoxin.
We showed that overexpression of TRXs reduced cell death; TRX2 was expressed in the mitochondria, while TRX1 was expressed in the cytoplasm.
knockdown of TRX-1 or TRX-2 sensitizes cells to CYP2E1-induced oxidant stress partially via ASK-1 and JNK1 signaling pathways. Both TRX-1 and TRX-2 are important for defense against CYP2E1-induced oxidative stress.
Data show that knockdown of S100P led to downregulation of thioredoxin 1 and beta-tubulin and upregulation of RhoGDIA, all potential therapeutic targets in cancer.
TRX1 and TRX2 regulate the proliferation and survival of adipocyte derived stem cells; these processes are mediated by the activation of ERK1/2
Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.
mitochondrial thioredoxin may play important roles in protection against oxidant-induced apoptosis
MT-TRX has a role in the regulation of the mitochondrial membrane potential and cell death
Thioredoxin 1 and thioredoxin 2 have opposed regulatory functions on hypoxia-inducible factor-1alpha.
The additive protection by Trx2 and GSH shows that Trx2 and GSH systems are both functionally important at low oxidative stress conditions.
The LC/ICPMS analyses showed that the trivalent arsenic species were able to form complexes with both human and E. coli Trx.
upon stimulation of Fas, thioredoxin-2 mediated denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis
This is the first demonstration of biochemical and physiological consequences caused by loss of Trx-2 in Drosophila.
gene for thioredoxin (DmTrx-2) was cloned and expressed, and the protein characterized
Drosophila thioredoxin can function as an anti-aging agent and as a suppressor of Parkin-associated endothelin receptor-like receptor - and poly-glutamine-induced neurotoxicity
Trx-2 affects lifespan in Drosophila. Mutants have a decreased lifespan.
Loss of TXN2 alters mitochondrial respiratory function and induces cardiomyocyte hypertrophy.
The ventral signal observed from early stages colocalized with motor neuron markers Isl1/2 and FoxP1 and the strong ventral signal colocalizing with Isl1/2 was observed in all rostrocaudal segments of the spinal cord.
TRX-2 overexpression does not mitigate adverse effects of a high-calorie diet on synaptic plasticity
An essential role was identified for thioredoxin-2 in preserving cardiac function by suppressing mitochondrial reactive oxygen species.
The SirT1 regulates the expression of several antioxidant genes in bovine aortic endothelial cells, including Mn superoxide dismutase, catalase, peroxiredoxins 3 and 5, thioredoxin 2, thioredoxin reductase 2, and uncoupling protein 2.
This study shows that both fructose and glucose-sweetened liquid consumption results in fatty liver and upregulated thioredoxin-2 expression.
Data show that Nrf2 activity was increased in WT MEFs at the 0 or -46 mV conditions, but was inhibited in Trx2 Tg MEFs under the same conditions.
Homozygous mutant embryos do not survive to birth and die after implantation at Theiler stage 15/16.
the rapid E2-mediated activation of the Txn pathway is an important step in the response of the mammalian uterus to estrogen.
Trx2 is an endogenous regulator of the mitochondrial permeability transition.
This nuclear gene encodes a mitochondrial member of the thioredoxin family, a group of small multifunctional redox-active proteins. The encoded protein may play important roles in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis.
, thioredoxin, mitochondrial
, thioredoxin 2
, Thioredoxin 2
, thioredoxin nuclear gene encoding mitochondrial protein