PRDX2 Mouse Monoclonal Antibody
These results show that Prdx2 is upregulated in gastric cancer and may play a role in its pathogenesis. To determine this, we used the Kaplan-Meier Plotter to stratify gastric cancer based on Prdx2 into high and low. Prdx2 probes included _x_at (auto cutoff value used 265; Figure 7D) and _at (auto cutoff value used 145; Figure 7E). Results show a strong association between high Prdx2 expression and low 5-year survival of patients (Figure 7D & E).
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].
The serum which is used should match the species of the secondary antibody. Diao S, Zhang JF, Wang H, He ML, Lin MC, Chen Y, Kung HF. Proteomic identification of microRNA-122a target proteins in hepatocellular carcinoma. Kim K, Yu M, Han S, Oh I, Choi YJ, Kim S, Yoon K, Jung M, Choe W. Expression of human peroxiredoxin isoforms in response to cervical carcinogenesis. Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ. Overexpression of peroxiredoxin in human breast cancer. Oxidative stress and redox regulation of gametogenesis, fertilization, and embryonic development.
As shown in Figure 12, forced expression of PRDX2-V5 or PRDX4-V5 did not alter HIF-1α-p300 interaction in hypoxic HeLa cells. Thus, PRDX2 and PRDX4 do not inhibit the recruitment of p300 to HIF-1α. Next, we studied whether PRDX family members interact with HIF-2α in cells. As shown in Figure 1D, PRDX2-V5 and PRDX4-V5 strongly bound to endogenous HIF-2α in hypoxic HeLa cells, whereas PRDX1-V5 and PRDX3-V5 weakly interacted with endogenous HIF-2α. No interaction of HIF-2α with PRDX5-V5 or PRDX6-V5 was detectable in hypoxic HeLa cells.
If the antibody doesn’t perform, you can receive a hassle-free refund or credit note. Representative images of PRDX2 and p-AKT expression in human colon carcinoma samples and normal adjacent tissues are shown. Based on PCR analysis of DNAs from a human/rodent somatic cell hybrid panel, Pahl et al. assigned the TDPX1 locus to chromosome 13. Further localization to 13q12 was achieved by fluorescence in situ hybridization, using as a probe DNA from a YAC that contained the TDPX1 gene. However, Gross mapped the PRDX2 gene to chromosome 19p13.2 based on an alignment of the PRDX2 sequence with the genomic sequence .
Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression. PRDX2 also known as NKEFB, PRP, PRX2, PRXII or TPX1, is a protein that in humans is encoded by the PRDX2 gene. This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells.
We also demonstrate that PRDX2 is a direct HIF target gene and that PRDX2 expression is induced by prolonged hypoxia. These findings uncover a novel feedback mechanism for inhibition of HIF transcriptional activity under conditions of prolonged hypoxia. The present study demonstrates that mammalian spermatozoa and seminal plasma possess PRDX2 protein. The sperm redox system is functionally active and potentially has an important role in protecting spermatozoa from ROS in the female reproductive milieu until fertilization is ensured.
Therefore, we analyzed the expression of MAPK signaling-related proteins in sh-PRDX2 cells. The protein levels of phospho-P38 MAPK were significantly decreased in PRDX2-knockdown cells, though levels of p-JNK and p-ERK did not appear to be significantly affected . These results indicate that PRDX2 acts via the P38/FOXO pathway to regulate cell-cycle progression and autophagy flux.
Rely on Thermo Scientific Nalgene Rapid Flow Filtration Units See how the unique Nalgene Rapid-Flow membrane support system provides the last line of defense against contamination. We are committed to providing you with products and processes that make it easy for you to focus on results... Quanta Biosciences and VWR are proud to fund a grant award for publication of research involving qPCR methodologies utilizing any Quanta Bioscience qPCR reagent in JoVE.
These results suggest that depleting PRDX2 combined with 5-FU treatment could be a promising strategy for anticancer drug resistance. To ascertain the effect of PRDX2 knockdown in colon tumor growth, we examined the in vivo efficacy of 5-FU in mice bearing abdominal tumors that originated from HCT116-shPRDX2 or HCT116-shCont cells. Using Kaplan–Meier analysis with the log-rank test, we found that the mice in the shCont group treated with 5-FU and the untreated shPRDX2 group had longer survival times than the mice in the untreated shCont group. However, the mice in the shPRDX2 group treated with 5-FU exhibited the longest survival time of the four groups . These in vivo results suggest that PRDX2 contributes to anticancer drug resistance and that decreasing the expression of PRDX2 in combination with 5-FU treatment reduces tumor development in colon cancer.
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.
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].
The serum which is used should match the species of the secondary antibody. Diao S, Zhang JF, Wang H, He ML, Lin MC, Chen Y, Kung HF. Proteomic identification of microRNA-122a target proteins in hepatocellular carcinoma. Kim K, Yu M, Han S, Oh I, Choi YJ, Kim S, Yoon K, Jung M, Choe W. Expression of human peroxiredoxin isoforms in response to cervical carcinogenesis. Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ. Overexpression of peroxiredoxin in human breast cancer. Oxidative stress and redox regulation of gametogenesis, fertilization, and embryonic development.
As shown in Figure 12, forced expression of PRDX2-V5 or PRDX4-V5 did not alter HIF-1α-p300 interaction in hypoxic HeLa cells. Thus, PRDX2 and PRDX4 do not inhibit the recruitment of p300 to HIF-1α. Next, we studied whether PRDX family members interact with HIF-2α in cells. As shown in Figure 1D, PRDX2-V5 and PRDX4-V5 strongly bound to endogenous HIF-2α in hypoxic HeLa cells, whereas PRDX1-V5 and PRDX3-V5 weakly interacted with endogenous HIF-2α. No interaction of HIF-2α with PRDX5-V5 or PRDX6-V5 was detectable in hypoxic HeLa cells.
If the antibody doesn’t perform, you can receive a hassle-free refund or credit note. Representative images of PRDX2 and p-AKT expression in human colon carcinoma samples and normal adjacent tissues are shown. Based on PCR analysis of DNAs from a human/rodent somatic cell hybrid panel, Pahl et al. assigned the TDPX1 locus to chromosome 13. Further localization to 13q12 was achieved by fluorescence in situ hybridization, using as a probe DNA from a YAC that contained the TDPX1 gene. However, Gross mapped the PRDX2 gene to chromosome 19p13.2 based on an alignment of the PRDX2 sequence with the genomic sequence .
Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression. PRDX2 also known as NKEFB, PRP, PRX2, PRXII or TPX1, is a protein that in humans is encoded by the PRDX2 gene. This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells.
We also demonstrate that PRDX2 is a direct HIF target gene and that PRDX2 expression is induced by prolonged hypoxia. These findings uncover a novel feedback mechanism for inhibition of HIF transcriptional activity under conditions of prolonged hypoxia. The present study demonstrates that mammalian spermatozoa and seminal plasma possess PRDX2 protein. The sperm redox system is functionally active and potentially has an important role in protecting spermatozoa from ROS in the female reproductive milieu until fertilization is ensured.
Therefore, we analyzed the expression of MAPK signaling-related proteins in sh-PRDX2 cells. The protein levels of phospho-P38 MAPK were significantly decreased in PRDX2-knockdown cells, though levels of p-JNK and p-ERK did not appear to be significantly affected . These results indicate that PRDX2 acts via the P38/FOXO pathway to regulate cell-cycle progression and autophagy flux.
Rely on Thermo Scientific Nalgene Rapid Flow Filtration Units See how the unique Nalgene Rapid-Flow membrane support system provides the last line of defense against contamination. We are committed to providing you with products and processes that make it easy for you to focus on results... Quanta Biosciences and VWR are proud to fund a grant award for publication of research involving qPCR methodologies utilizing any Quanta Bioscience qPCR reagent in JoVE.
These results suggest that depleting PRDX2 combined with 5-FU treatment could be a promising strategy for anticancer drug resistance. To ascertain the effect of PRDX2 knockdown in colon tumor growth, we examined the in vivo efficacy of 5-FU in mice bearing abdominal tumors that originated from HCT116-shPRDX2 or HCT116-shCont cells. Using Kaplan–Meier analysis with the log-rank test, we found that the mice in the shCont group treated with 5-FU and the untreated shPRDX2 group had longer survival times than the mice in the untreated shCont group. However, the mice in the shPRDX2 group treated with 5-FU exhibited the longest survival time of the four groups . These in vivo results suggest that PRDX2 contributes to anticancer drug resistance and that decreasing the expression of PRDX2 in combination with 5-FU treatment reduces tumor development in colon cancer.
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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