The Journaling of Olsen 368

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. In Western blots, approximately 25%-40% cross-reactivity with recombinant human Peroxiredoxin 1 and 4 is observed, and less than 10% cross-reactivity with rhPeroxiredoxin 3, 5, and 6 is observed. In direct ELISAs, approximately 15%-25% cross-reactivity with rhPeroxiredoxin 1 and 4 is observed, and less than 5% cross-reactivity with rhPeroxiredoxin 3, 5, or 6 is observed.
Our results show that bio-Celastrol binds to Prdx2 protein in lysates from both gastric cancer cells in culture and gastric cancer tissues generated in mice (Figure 3I & J). These data indicate that Celastrol can directly bind to Prdx2 protein with high affinity. Increasing ROS in cancer cells that overwhelms the antioxidant clearance has been reported to induce apoptosis through a series of downstream pathways, such as endoplasmic reticulum genways PRDX2 antibody stress and mitochondrial cascade . Several drugs with cancer-targeting properties such as trisenox , paclitaxel , and 2-methoxyestradiol have been shown to increase ROS levels. Based on these findings, drugs that regulate cellular redox proteins may offer avenues for cancer treatment. Prdx proteins (Prdx 1-6) are abundant thiol-dependent peroxidases that reduce hydrogen peroxide, peroxynitrite, and other hydroperoxides [8-10].

DHE staining showed that NAC inhibited Celastrol-increased ROS level in tumor tissues . Cisplatin, used as a positive control, increased ROS levels and reduced gastric cancer growth in mice. Celastrol is a bioactive constituent extracted from Tripterygium wilfordii, a traditional Chinese medicinal herb [16-18]. Although the mechanisms underlying this inhibitory activity are not fully clear, recent studies found that Celastrol increased ROS levels several-fold and caused cell cycle arrest, apoptosis, and autophagy in cancer cells .
Even though 1 mg/kg dose was effective in reducing tumor growth, 2 mg/kg Celastrol completely prevented it. These effects were seen without changes to body weights of mice treated with Celastrol or histological assessment of pathological changes in heart, kidneys, and livers of mice . Analysis of harvested tumor specimens showed increased DHE staining indicative of elevated levels of ROS in Celastrol-treated mice .

We have listed RNA Seq and gene expression data in the "Target Info" tab. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human PRDX2 protein. Antibodies are purified by protein A and peptide affinity chromatography. Cells were seeded in 96-well plates at 1 × 104 cells per well in RPMI 1640 medium with 10% FBS and treated with 0, 2.5, 5, 10, 20, 40 and 80 μg/ml of 5-FU (Cayman Chemical, Ann Arbor, Michigan, U.S.A.) for 48 h. The viability of cells was evaluated using the Cell Counting Kit-8 (CCK-8) assay (Dojindo Laboratories, Minato-ku, Tokyo, Japan), according to the manufacturer’s instructions.
Cancer cells exposed to prolonged hypoxia are more aggressive and resistant to radiation and chemotherapy, and differential gene expression is likely to contribute to this phenotype . It will be interesting to determine if PRDX2 and PRDX4 regulate the aggressive phenotype of cancer cells under prolonged hypoxia. Gene in endothelial cells, thereby potentiating VEGF expression . Regulation of HIF activity by PRDX2 or PRDX4 has not been reported. HIFs are heterodimeric transcription factors consisting of α and β subunits .

The oxidized PRDX are reverted to their active reduced state by the electrons donated by NADPH via the TRX system composed of TRX reductase and TRX. Immunoprecipitation with PRDX2 antibody pulled out three other proteins, namely, GPX4, SMCP, and CNBP, along with PRDX2 itself. Among them, GPX4 and SMCP are known to be multifunctional proteins responsible for the structural integrity of the mitochondrial sheath in mature spermatozoa. Biochemical affinity of PRDX2 to GPX4 and SMCP and their colocalization in the mitochondrial sheath strongly suggest that these three proteins might functionally interact to form the mitochondrial sheath.
However, PRDX2 knockdown showed no effects on the basal level of cell death (Fig. 4A and B). Taken together, these data suggest that PRDX2 antagonizes TNF-α-induced apoptosis in SMMC-7721 cells. In our study, we used PRDX2-shRNA-LV to deplete PRDX2 expression in colon cancer cells. We showed that knocking down PRDX2 in vitro facilitates cell death and apoptosis in colon cancer cells treated with 5-FU. In addition, PRDX2 depletion in vivo in combination with 5-FU treatment, markedly inhibited tumor growth compared with treatment with 5-FU alone. Furthermore, we found that the PI3K/AKT signaling pathway plays a role in 5-FU-induced apoptosis in colon cancer.
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The tumor suppressor p53 also binds to HIF-1α and induces MDM2-dependent ubiquitination and proteasomal degradation of HIF-1α . Finally, HIF-1α is also subject to lysosomal degradation through chaperone-mediated autophagy, which is mediated by binding of HSC70 and LAMP2A . Moon JC, Hah YS, Kim WY, Jung BG, Jang HH, Lee JR, Kim SY, Lee YM, Jeon MG, Kim CW, et al. Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. O'Neill et al. showed that nontranscriptional mechanisms are sufficient to sustain circadian timekeeping in the eukaryotic lineage, although they normally function in conjunction with transcriptional components. They identified oxidation of peroxiredoxin proteins as a transcription-independent rhythmic biomarker, which is also rhythmic in mammals.
The catalytically inactive PRDX2 and PRDX4 mutants were generated using QuickChange Site-directed Mutagenesis Kit . PRDX2 and PRDX4 shRNA oligonucleotides were ligated into Teton-pLKO (Addgene #21915). The DNA sequences of all recombinant plasmids were confirmed by nucleotide sequence analysis. WCL was subject to IP with anti-p300 antibody, followed by immunoblot assays using antibodies against HIF-1α, V5, and p300.