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Human Polyclonal PRDX3 Primary Antibody for IF (p), IHC (p) - ABIN735713
Gao, Liu, Chen, Lv, Wu, Mi, Wang: Comparative study of Hsp27, GSK3?, Wnt1 and PRDX3 in Hirschsprung's disease. in International journal of experimental pathology 2014
Human Monoclonal PRDX3 Primary Antibody for IP, WB - ABIN534426
Wood, Schröder, Robin Harris, Poole: Structure, mechanism and regulation of peroxiredoxins. in Trends in biochemical sciences 2003
Human Polyclonal PRDX3 Primary Antibody for IF, WB - ABIN524344
Liu, Rong, Li, Liu, Wang, Li: Vasectomy induces oxidative stress and up-regulates the expression of peroxiredoxins in mouse testis in short and early periods after surgery. in The Journal of urology 2014
Human Polyclonal PRDX3 Primary Antibody for IF, WB - ABIN524343
Kannan, Nguyen, Makarem, Dong, Shih, Eirew, Raouf, Emerman, Eaves: Glutathione-dependent and -independent oxidative stress-control mechanisms distinguish normal human mammary epithelial cell subsets. in Proceedings of the National Academy of Sciences of the United States of America 2014
the role of Spalt like protein 4 (SALL4) in pancreatic ductal adenocarcinoma cell proliferation, mobility and its regulation in mitochondrial ROS via FoxM1/Prx III axis.
tubular PRX3 in combination with conventional predictors can further improve recovery prediction and may help with risk stratification in AKI patients with pre-existing CKD.
results suggest that decreased PRDX3 by excessive bile acids in trophoblasts plays a critical role in the pathogenesis and progression of Intrahepatic cholestasis of pregnancy.
Mutants created to investigate link between oligomerisation and peroxidase activity. Obligate dimer is less active than wildtype but still displays peroxidase activity. 2.4A structure (PDB: 5UCX) shows cysteine-stabilised protein interface.
the present study identified the protein profiles of the PRDX family in LSCC and showed that down-regulation of PRDX3 in Hep-2 cells induced cell apoptosis and inhibited cell proliferation and cell migration.
The UNG1-PRDX3 interaction protected UNG1 from reactive oxygen species-mediated degradation and prevented mitochondrial DNA oxidation.
PRDX3 knockdown led to the down-regulation of ATP synthases and the decreased cellular ATP level, contributing to the slow-down of cell growth. Furthermore, silencing PRDX3 enhanced invasive properties of HepG2 cells via TIMP-1 down-regulation and the increased ECM degradation
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
PRX3 plays a crucial role in mitochondrial homeostasis.
High PRX3 expression is associated with invasion of lung adenocarcinoma.
We also found that forkhead box protein 1 (FOXM1)-induced peroxiredoxin 3 (PRDX3) maintains the mitochondrial function, and the FOXM1/PRDX3 mitochondrial pathway maintains survival of colon CSCs
Oxidative stress promotes PRX2 and PRX3 hyperoxidation and attenuates pro-survival signaling in aging chondrocytes.
the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3. Reduction and re-oxidation of the hyperoxidized dimer of Prx3 produced hyperoxidized monomers
Data indicate that peroxiredoxin III (PrxIII) is a common direct target of both miroRNAs miR-26a-5p and miR-23b-3p.
Colon cancer stem cells overexpress the mitochondrial gene PRX3, which is required for maintenance of mitochondrial function and tumorigenesis, and is regulated by forkhead box protein 1, which also regulates expression of CD133 in these cells.
High serum PRDX3 levels are associated with hepatocellular carcinoma.
Peroxiredoxin 3 levels regulate a mitochondrial redox setpoint in malignant mesothelioma cells.
two placental proteins, Prx3 and Prx4, may act as new placental immune targets.
Serum PRDX3 can be used as a noninvasive biomarker for the diagnosis and/or prognosis of hepatocellular carcinoma.
High peroxiredoxin 3 protein expression is associated with hepatocellular carcinoma.
The importance of mitochondrial Prdx3 in regulating the oxidative stress environment in adipocytes.Loss of Prdx3 leads to decreased pS473 Akt and insulin-stimulated glucose transport.
This study showed that from E10.5,Prdx3 showed strong ventral lateral expression. This increased ventral immunotaining persisted until E18.5 but became relatively less striking at later stages.
Prx3 plays a crucial role in mitochondrial homeostasis and thereby controls the contractile functions of skeletal muscle.
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.
Prx3 is up-regulated in response to oxidative stress; the maintenance of Prx3 levels in hair cells is a critical factor in their susceptibility to acquired hearing loss.
The concerted action of PrxIII and Srx is important for protection against pyrazole-induced oxidative stress arising from the convergent induction of CYP2E1-derived and ER stress-derived ROS in mitochondria.
PrxIII in mouse adrenal cortex is inactivated by H(2)O(2) produced by cytochrome P450 enzymes during corticosterone production stimulated by adrenocorticotropic hormone.
endogenous Prx3 may play an essential role in maintaining normal characteristics of adipocytes and that defect in Prx3 alters mitochondrial redox state and function.
Immunohistochemical analysis revealed segment-specific alterations induced by the ischemic insult. Grx2, Prx3, and Prx6 were highly expressed in proximal tubule cells
Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.
Results indicate that PrxIII is not involved in pre-eclamptic development. Instead, PrxIII is an indispensable antioxidant in placentas where oxidative stress exists.
This study showed that peroxiredoxin 3 protects pancreatic beta cells from cell stress induced by accumulation of hydrogen peroxide, or the induction of inducible nitric oxide synthase or caspase-9 and -3 by pro-inflammatory cytokines or streptozotocin.
Hyperoxia induced the degradation of Prx III in Nrf2-deficient mice but not in wild-type animals, suggesting that, in the absence of a sufficient amount of Srx
PRDX3 is a c-Myc target gene that is required to maintain normal mitochondrial function. c-Myc directly activates expression of a mitochondrial peroxiredoxin that is required for Myc-mediated transformation.
mitochondrial Prdx3 is an important cellular antioxidant that regulates physiological levels of H(2)O(2)
Roles of MER5 function for the oxidative stress responses by intratracheal inoculation of lipopolysaccharide (LPS) to the mice were examined.
Expression of 40 proteins, including the antioxidative enzymes peroxiredoxin 1 and 3, glutathione peroxidase 1, and SOD-1, was increased with diabetes, suggesting an adaptive response to oxidative stress associated with this diabetic model.
significantly increased following 200 microM mono-(2-ethylhexyl) phthalate treatment
Nitrosative stress leads to protein glutathiolation, increased s-nitrosation, and up-regulation of Prx VI, but not Prx II or Prx III in the heart
Data suggest that during ectogenesis of blastocysts infected with bovine Herpesvirus type 5, expression of AOP-1 is induced; this effect may be involved in inhibition of apoptosis in infected blastocysts/embryos.
PRDX3, also known as SP-22, is a mitochondrial 2-CYS peroxiredoxin organized as a decameric toroid
This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.
thioredoxin-dependent peroxide reductase, mitochondrial
, peroxiredoxin 3
, mitochondrial thioredoxin-dependent peroxide reductase
, antioxidant protein 1
, peroxiredoxin III
, protein MER5 homolog
, Prx III
, anti-oxidant protein 1
, antioxidant protein
, mitochondrial Trx dependent peroxide reductase
, mitochondrial thioredoxin dependent peroxide reductase
, PRx III
, 5'-methylthioadenosine phosphorylase
, MTA phosphorylase
, anti-oxidant like protein-1