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Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Additionally we are shipping Sulfiredoxin 1 Kits (4) and Sulfiredoxin 1 Proteins (2) and many more products for this protein.
Showing 10 out of 35 products:
Human Polyclonal SRX1 Primary Antibody for IF (p), IHC (p) - ABIN1387599
Zhou, Zhou, Yu, Wu, Chen, Zhao et al.: Sulfiredoxin-1 exerts anti-apoptotic and neuroprotective effects against oxidative stress-induced injury in rat cortical astrocytes following exposure to oxygen-glucose deprivation and hydrogen ... in International journal of molecular medicine 2015
Human Polyclonal SRX1 Primary Antibody for ELISA, WB - ABIN450073
Jönsson, Johnson, Lowther: Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. in Nature 2008
We silenced Srx by short hairpin RNA in HeLa and SiHa cells. Diminished Srx expression upregulated E-cadherin (show CDH1 Antibodies) expression. The cell invasion and migration activity in the ShSrx group were obviously decreased in HeLa and SiHa cells.
Study shows that Srx plays a critical oncogenic role to promote cell invasion and metastasis, which is at least partially due to its stimulation of the MAPK (show MAPK1 Antibodies) pathway through EGFR (show EGFR Antibodies) deacetylation.
This review will summarize the molecular basis of differences in the affinity of Srx for individual Prx (show PRDX6 Antibodies) and the role of individual component of the Srx-Prx (show PRDX6 Antibodies) system in tumor progression and metastasis.
Gemfibrozil, a lipid-lowering drug, increases myelin genes in human oligodendrocytes via peroxisome proliferator-activated receptor-beta (show PPARD Antibodies).
NRF2 (show GABPA Antibodies) and SRXN1 genetic polymorphisms are associated with breast cancer risk and survival
SRX forms a complex with S100A4 (show S100A4 Antibodies) (and has stronger affinity for S-glutathionylated S100A4 (show S100A4 Antibodies)), regulates its activity, and mediates redox regulation of the interaction of S100A4 (show S100A4 Antibodies) with nonmuscle myosin heavy chain II-A (show MYH9 Antibodies).
Srx functions as a novel component to maintain the balance between H2O2 production and elimination
Real-time PCR validated that up-regulation of sulphiredoxin 1 homolog (SRXN1), hemeoxygenase 1 (HMOX1), and breast carcinoma amplified sequence 3 (BCAS3) were consistently modulated.
Srx-Prx IV (show PRDX4 Antibodies) axis is critical for lung cancer maintenance and metastasis, suggesting that targeting the Srx-Prx IV (show PRDX4 Antibodies) axis may provide unique effective strategies for cancer prevention and treatment.
sulfiredoxin 1 is associatd with the pathogenesis of human pulmonary fibrosis.
sulfiredoxin is degraded by Lon (show LONP1 Antibodies) in a manner dependent on PrxIII (show PRDX3 Antibodies) hyperoxidation state.
Srx is one of the critical components that contribute to mouse skin tumorigenesis in vivo.
data provide in vivo evidence that loss of Srx renders mice resistant to azoxymethane/dextran sulfate sodium-induced colon carcinogenesis, suggesting that Srx has a critical oncogenic role in cancer development
The concerted action of PrxIII (show PRDX3 Antibodies) and Srx is important for protection against pyrazole-induced oxidative stress arising from the convergent induction of CYP2E1 (show CYP2E1 Antibodies)-derived and ER stress-derived ROS (show ROS1 Antibodies) in mitochondria.
NO-mediated Srx up-regulation is mediated by the transcription factor nuclear factor erythroid 2-related factor (Nrf2 (show NFE2L2 Antibodies)) and the NO/Srx pathway inhibits generation of reactive oxygen species.
LPS (show TLR4 Antibodies)-mediated Srx induction is dependent on both AP-1 (show JUN Antibodies) and Nrf2 (show NFE2L2 Antibodies), which is regulated by Nox2 (show CYBB Antibodies)-derived reactive oxygen species.
Synaptic activity upregulated the thioredoxin (show TXN Antibodies)-peroxiredoxin reactivating gene sulfiredoxin.
Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.
, sulfiredoxin 1 homolog
, sulfiredoxin 1 homolog (S. cerevisiae)
, neoplastic progression 3
, neoplastic progression protein 3