PRDX2 Human Recombinant Protein
Stresing V, Baltziskueta E, Rubio N, Blanco J, Arriba MC, Valls J, Janier M, Clézardin P, Sanz-Pamplona R, Nieva C, et al. Peroxiredoxin 2 specifically regulates the oxidative and metabolic stress response of human metastatic breast cancer cells in lungs. Transcript and protein analysis reveals better survival skills of monocyte-derived dendritic cells compared to monocytes during oxidative stress. Our bioprocessing products are engineered to the highest quality standards and regulatory requirements. Explore our solutions for multiple applications - vaccines, monoclonal antibodies, recombinant proteins, cell or gene therapy.
We analyzed the cell apoptosis by flow cytometry and found that knocking down PRDX2 expression in FU-treated colon cancer cells markedly increased apoptosis and protein levels of cleaved PARP and caspase-3 . Collectively, our results suggest that PRDX2 depletion, combined with 5-FU, promotes cell apoptosis in colon cancer cells. To investigate the role of PRDX2 in colon genways PRDX2 antibody cancer cells, we transfected PRDX2-shRNA-LV and NC-shRNA-LV into the HT-29 and HCT116 cell lines. The mRNA and protein expressions of PRDX2 were significantly decreased in the shPRDX2 group compared with the shCont group . These results demonstrate that the lentivirus-mediated shRNA targetted PRDX2 effectively and knocked down PRDX2 expression in colon cancer cells.
To further evaluate the functions of the 173 genes, we performed KEGG enrichment analysis using RStudio . Among the top 10 differentially expressed pathways, the FOXO pathway was the second most significantly enriched . Notably, p38 MAPK was identified within this pathway as a significantly differentially expressed gene. These results raise the possibility that PRDX2 may regulate cell-cycle progression and autophagy in CRC through the p38/FOXO pathway. Human NPC CNE2 cell proteins were separated by 2-DE, and transferred onto PVDF membranes or visualized by silver staining (Fig.1d). The membranes were screened individually from 7 NPC patients and from 7 matched normal controls to identify the presence of autoantibodies against candidate antigens from CNE2 cells.
Pylori induces PRDX2 expression, protecting gastric mucosa against reactive oxygen species, oxidative DNA damage and DNA double-strand breaks. We are continuously updating our ELISA Kit catalog with advanced verified products. If you can not download the datasheet please send your request of our latest datasheet. These standard curves of E2925Hu are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
Levels of malondialdehyde , products of polyunsaturated fatty acid peroxidation, were also increased by Celastrol, confirming increased oxidative stress . As identified in our in vitro studies, we measured the Prdx activity in tumor tissue lysates and show supressed levels upon treatment of mice with Celastrol . These results support the notion that Celastrol binds to Prdx2 protein and inhibits its activity. Supressed Prdx activity and enhanced ROS levels by Celastrol correlated with increased levels of cleaved-caspase 3 and ER stress protein CHOP (Figure 5G & H), as well as reduced tumor cell ki-67 immunoreactivity .
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight. In HT-29 cells, the shCont group and shPRDX2 group were exposed to 5-FU for 48 h and cell viability was measured by the CCK-8 assay. In HCT116 cells, the shCont group and shPRDX2 group were exposed to 5-FU for 48 h and cell viability was measured by the CCK-8 assay.
Iodoacetamide was added at a final concentration of 10 mM and incubated at RT for 30 min in the dark. After rehydrated, the gel particles were incubated with trypsin solution (10 μg/ml in 50 mM ammonium bicarbonate) at 37 °C overnight. The in-gel digests were extracted and concentrated to complete dryness using the SpeedVac and stored at −20 °C. Approval for the study from the institutional ethics review committee center was obtained, and written informed consents were obtained from all patients and normal controls. We thank Beverly DaGue of the Charles Gehrke Proteomics Center, University of Missouri, for MS analysis.
To verify the role of PI3K/AKT in PRDX2-induced drug resistance, we treated HT-29 cells with the AKT inhibitor, MK HCl and then observed the resistance of HT-29 cells to 5-FU. However, elevated expressions of caspase-3 and Bax were detected, along with suppressed Bcl-2 expression post MK-2206 treatment . These results were validated by measuring apoptosis by using flow cytometry after cells were treated 5-FU in the presence or absence of MK-2206 HCl. We observed higher C-PARP and Bax protein expression and a higher rate of apoptosis in colon cancer cells treated with MK HCl . Together, these data suggest that 5-FU targets PRDX2 and down-regulates its expression through the AKT/PI3K pathway.
Related pseudogenes have been identified on chromosomes 5, 6, 10 and 13. Hwang et al. found that 5-FU treatment induced ROS generation in human lung carcinoma cells, leading to a higher level of antioxidant enzymes and resistance to 5-FU. PRDX proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity .
To explore whether PRDX2 expression regulates the cell cycle in CRC cells, we introduced PRDX2-shRNA into HCT116 and HT29 cell lines and evaluated proliferation using a cell-counting kit (CCK-8) assay. The data suggest that PRDX2 knockdown suppresses CRC cell proliferation . Furthermore, flow cytometry results indicate that PRDX2 knockdown causes cell-cycle arrest in S phase . Western blot analysis demonstrated that sh-PRDX2 upregulates the expression of the cell-cycle markers P21 and P27 in both HCT116 and HT29 cell lines . However, high expression of PRDX2 did not significantly affect the cell cycle . These results indicated that PRDX2 plays a critical role in maintaining CRC cell-cycle progression.
The prominent peaks of the Nanospray Qq-TOF MS/MS spectrum of the 20- to 23-kDa band of the anti-PRDX2 immunoprecipitated boar seminiferous tubule extract. Control Western blotting was performed using immunoadsorbed antibody. Two micrograms of anti-PRDX2 antibody was incubated with 3 μg of human recombinant PRDX2 protein (protein stock [1 mg/ml]) in 10 ml of TBS-Tween with 1% nonfat milk for 1 h. The neutralized antibody solution was used for Western blotting of various extracts following the standard protocol. Normal sera for immunohistochemistry applications are available as neat serum for blocking reagents.
We analyzed the cell apoptosis by flow cytometry and found that knocking down PRDX2 expression in FU-treated colon cancer cells markedly increased apoptosis and protein levels of cleaved PARP and caspase-3 . Collectively, our results suggest that PRDX2 depletion, combined with 5-FU, promotes cell apoptosis in colon cancer cells. To investigate the role of PRDX2 in colon genways PRDX2 antibody cancer cells, we transfected PRDX2-shRNA-LV and NC-shRNA-LV into the HT-29 and HCT116 cell lines. The mRNA and protein expressions of PRDX2 were significantly decreased in the shPRDX2 group compared with the shCont group . These results demonstrate that the lentivirus-mediated shRNA targetted PRDX2 effectively and knocked down PRDX2 expression in colon cancer cells.
To further evaluate the functions of the 173 genes, we performed KEGG enrichment analysis using RStudio . Among the top 10 differentially expressed pathways, the FOXO pathway was the second most significantly enriched . Notably, p38 MAPK was identified within this pathway as a significantly differentially expressed gene. These results raise the possibility that PRDX2 may regulate cell-cycle progression and autophagy in CRC through the p38/FOXO pathway. Human NPC CNE2 cell proteins were separated by 2-DE, and transferred onto PVDF membranes or visualized by silver staining (Fig.1d). The membranes were screened individually from 7 NPC patients and from 7 matched normal controls to identify the presence of autoantibodies against candidate antigens from CNE2 cells.
Pylori induces PRDX2 expression, protecting gastric mucosa against reactive oxygen species, oxidative DNA damage and DNA double-strand breaks. We are continuously updating our ELISA Kit catalog with advanced verified products. If you can not download the datasheet please send your request of our latest datasheet. These standard curves of E2925Hu are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
Levels of malondialdehyde , products of polyunsaturated fatty acid peroxidation, were also increased by Celastrol, confirming increased oxidative stress . As identified in our in vitro studies, we measured the Prdx activity in tumor tissue lysates and show supressed levels upon treatment of mice with Celastrol . These results support the notion that Celastrol binds to Prdx2 protein and inhibits its activity. Supressed Prdx activity and enhanced ROS levels by Celastrol correlated with increased levels of cleaved-caspase 3 and ER stress protein CHOP (Figure 5G & H), as well as reduced tumor cell ki-67 immunoreactivity .
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight. In HT-29 cells, the shCont group and shPRDX2 group were exposed to 5-FU for 48 h and cell viability was measured by the CCK-8 assay. In HCT116 cells, the shCont group and shPRDX2 group were exposed to 5-FU for 48 h and cell viability was measured by the CCK-8 assay.
Iodoacetamide was added at a final concentration of 10 mM and incubated at RT for 30 min in the dark. After rehydrated, the gel particles were incubated with trypsin solution (10 μg/ml in 50 mM ammonium bicarbonate) at 37 °C overnight. The in-gel digests were extracted and concentrated to complete dryness using the SpeedVac and stored at −20 °C. Approval for the study from the institutional ethics review committee center was obtained, and written informed consents were obtained from all patients and normal controls. We thank Beverly DaGue of the Charles Gehrke Proteomics Center, University of Missouri, for MS analysis.
To verify the role of PI3K/AKT in PRDX2-induced drug resistance, we treated HT-29 cells with the AKT inhibitor, MK HCl and then observed the resistance of HT-29 cells to 5-FU. However, elevated expressions of caspase-3 and Bax were detected, along with suppressed Bcl-2 expression post MK-2206 treatment . These results were validated by measuring apoptosis by using flow cytometry after cells were treated 5-FU in the presence or absence of MK-2206 HCl. We observed higher C-PARP and Bax protein expression and a higher rate of apoptosis in colon cancer cells treated with MK HCl . Together, these data suggest that 5-FU targets PRDX2 and down-regulates its expression through the AKT/PI3K pathway.
Related pseudogenes have been identified on chromosomes 5, 6, 10 and 13. Hwang et al. found that 5-FU treatment induced ROS generation in human lung carcinoma cells, leading to a higher level of antioxidant enzymes and resistance to 5-FU. PRDX proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity .
To explore whether PRDX2 expression regulates the cell cycle in CRC cells, we introduced PRDX2-shRNA into HCT116 and HT29 cell lines and evaluated proliferation using a cell-counting kit (CCK-8) assay. The data suggest that PRDX2 knockdown suppresses CRC cell proliferation . Furthermore, flow cytometry results indicate that PRDX2 knockdown causes cell-cycle arrest in S phase . Western blot analysis demonstrated that sh-PRDX2 upregulates the expression of the cell-cycle markers P21 and P27 in both HCT116 and HT29 cell lines . However, high expression of PRDX2 did not significantly affect the cell cycle . These results indicated that PRDX2 plays a critical role in maintaining CRC cell-cycle progression.
The prominent peaks of the Nanospray Qq-TOF MS/MS spectrum of the 20- to 23-kDa band of the anti-PRDX2 immunoprecipitated boar seminiferous tubule extract. Control Western blotting was performed using immunoadsorbed antibody. Two micrograms of anti-PRDX2 antibody was incubated with 3 μg of human recombinant PRDX2 protein (protein stock [1 mg/ml]) in 10 ml of TBS-Tween with 1% nonfat milk for 1 h. The neutralized antibody solution was used for Western blotting of various extracts following the standard protocol. Normal sera for immunohistochemistry applications are available as neat serum for blocking reagents.
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