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- Table of Contents
Facts about Peroxiredoxin-4.
Regulates the activation of NF-kappa-B in the cytosol by a modulation of I- kappa-B-alpha phosphorylation. .
Human | |
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Gene Name: | PRDX4 |
Uniprot: | Q13162 |
Entrez: | 10549 |
Belongs to: |
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peroxiredoxin family |
Antioxidant enzyme AOE372; AOE372; AOE37-2PRX-4; EC 1.11.1.15; Peroxiredoxin 4; Peroxiredoxin IV; peroxiredoxin-4; PRDX4; Prx4; prx-4; prx-IV; thioredoxin peroxidase (antioxidant enzyme); Thioredoxin peroxidase AO372; Thioredoxin-dependent peroxide reductase A0372
Mass (kDA):
30.54 kDA
Human | |
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Location: | Xp22.11 |
Sequence: | X; NC_000023.11 (23667493..23686397) |
Cytoplasm. Endoplasmic reticulum. Cotranslationally translocated to and retained within the endoplasmic reticulum. A small fraction of the protein is cytoplasmic.
Anti-Peroxiredoxin 4 (PRDX4) Markers are used in various applications. This article provides an overview of the applications and validation of the PRDX4 marker. It also discusses the high specificity and high affinity of this molecule. Boster Bio is committed to providing excellent quality antibodies to its customers. The company rewards its early reviewers with product credits. It also rewards scientists worldwide.
The antioxidant enzymes peroxiredoxins are a universal superfamily of antioxidant enzymes. They catalyze the reduction of all kinds of cellular peroxides and play a crucial role in cell proliferation, differentiation, and apoptosis. These enzymes are also highly expressed in various tissues, including the lung, tongue, and ovary.
The Boster Bio Anti-Peroxiredoxin 4/PDX4 Marker recognizes peptides that bind to peroxiredoxin 4. This antibody is available for WB applications. This anti-Peroxiredoxin 4/PRDX4 Marker is stored at -20°C for one year and 4°C for up to one month. It is made of 5mg BSA and 0.05mg thimerosal, and recognizes the 253-270aa sequence. For better results, you can also buy the blocking peptide.
In recent studies, PRDX6 was found to be overexpressed in cervical cancer cells. In fact, this protein suppressed cell apoptosis, which may be important for the growth of cervical cancer. Furthermore, it was found to inhibit cell migration and invasion. Therefore, the presence of PRDX6 could be a tumor promoter during the development and metastasis of cervical cancer.
PRDXs have been shown to play important roles in cellular homeostasis and disease development. Understanding these roles will allow the identification of new target therapeutic strategies. The PRDX4 gene has a broad range of applications, and these findings will aid in developing therapies for cancers. This article will review the current state of research on this gene and its applications in various cancer types. We will also discuss the future of this gene, and its future potential for use in targeted therapies.
As a nitro-oxidative stress protein, PRDX4 is expressed in cells and tissues. It is expressed in all three phylogenetic domains, including human, yeast, and plants. The gene is highly conserved and is composed of two subgroups based on sequence similarity. The prdx1/PRDX4 subgroup exhibits the broadest biological distribution, while the Prdx5 subgroup is missing in archaea.
Many cancers are associated with the expression of PRDX4 and a high number of PRDX4-positive cells. These cells are highly resistant to chemotherapy and may promote tumor recurrence. Furthermore, PRDX4 may protect tumor cells from ROS. Thus, studies suggest that PRDX4 may serve as a prognostic marker and a new drug. However, more research is needed to clarify its role in cancer progression.
Previous studies have shown that the PRDX4 gene may play an important role in lung cancer. In addition to its role in tumorigenesis, PRDX4 overexpression has been associated with increased levels of tumor-associated macrophages. This may explain the effect of PRDX4 on the tumor. However, we cannot rule out other factors, such as the presence of other cancer-related genes. The findings of the study show that PRDX4 overexpression can promote tumor development in various lung cancer models.
Validation with the PRDX4 marker provides a novel tool for the detection of gastric cancer. It is a multifunctional protein involved in several cellular functions and is known to play a role in tumor pathogenesis. Here, we discuss its potential as a biomarker and provide some evidence for its potential as a target. Here, we discuss its clinical and molecular functions in gastric cancer.
Peroxiredoxins play a vital role in male fertility. These antioxidant enzymes are present in both sperm and egg sperm. Only a few studies have examined their predictive capabilities. We used the PRDX4 marker as a biomarker in regression analysis. We found a significant positive correlation between PRDX4 and litter size. Furthermore, we demonstrated that PRDX4 was more predictive of fertility than other markers.
To validate the PRDX4 marker, we performed immunohistochemistry as described previously. Total proteins from HNSCC cell lines were extracted and transferred onto a 0.22-um PVDF membrane. The membrane was blocked with 5% non-fat skimmed milk. After blocking, 5 um sections were deparaffinized and analyzed using a Dako detection kit. After deparaffinizing, the slides were processed using OTTIX reagents. The antigen was then extracted using citrate buffer and pressure cooker.
In this validation, three different shRNA sequences targeting PRDX4 were constructed and transduced into HepG2 cells. Polybrene improved the transduction efficiency of the shRNAs. Of the three shRNAs tested, one was capable of achieving the required expression level. As a result, we have further validated the efficiency of transduction with the PRDX4 marker in our studies.
The expression of the PRDX4 marker is related to EGFR mutation status. Patients with both mutation and wild-type EGFR have a more favorable prognosis. This combination may represent a novel biomarker for prognosis. Mutation of the EGFR may inhibit PRDX4 from suppressing LUAD cell proliferation. This association between the PRDX4 and EGFR status could provide a new therapeutic target.
Researchers have identified PRDX4 as a potential biological marker for multiple diseases, including cancer. While its role in cancer is not fully understood, research has shown that overexpression of this protein facilitates tumor initiation, propagation, therapeutic resistance, and recurrence. Furthermore, increased levels of PRDXs have been found in numerous human cancers. While the exact mechanisms underlying PRDX4's role in cancer are still under investigation, it is thought that it serves as a new biomarker for various cancers.
The overexpression of PRDX4 may exacerbate the inflammatory and fibrotic changes that characterize IPF. It may also protect against future lung damage as it is an antioxidant enzyme. More research is needed to understand the precise role of PRDX4 in IPF. In addition to being a biomarker of IPF progression, the PRDX4 marker is associated with increased survival after lung transplantation.
In a study using human cells, the PRDX4 plasmid DNA was obtained from the Department of Pathology at Kagoshima University. Cells were cultured in growth media and transfected with 5 ug PRDX4 plasmid DNA duplexes using Life Technologies Lipofectamine(r) 2000. The PMCV-Tag-2b vector was used as a negative control.
The availability of the PRDX4 marker is a useful diagnostic tool to evaluate ER redox stress. This gene encodes the antioxidant enzyme peroxiredoxin-4. Loss of Prdx4 increases the pro-inflammatory potential of EVs, which are macrophage-derived cell-to-cell communication vehicles. This study provides new insights into the functions of EVs in inflammatory diseases.
The PRDX4-depleted group exhibited decreased proliferation. The PRDX4-rescue group showed increased protein expression and proliferation when compared with cells from the PRDX4-depleted groups. The PRDX4-rescue group had a higher percentage of cytokinesis-positive cells than PRDX4-depleted cells. The data was consistent and reproducible.
Availability of the PRDX4 marker in gastric cancer patients may be an accurate prognostic indicator of the cancer stage at diagnosis. It has been associated with several cellular functions, including a role in tumor growth and progression. The current study investigated whether PRDX4 is a viable prognostic biomarker for gastric cancer. If it is, it may represent a promising target biomarker for detecting gastric cancer.
Overexpression of PRDX4 in human lung cancer cells increased c-Jun phosphorylation and the expression of MMP9. Both overexpression and depletion of PRDX4 increased MMP9 levels in cancer cells. The increased MMP9 levels correlated with an increase in lung microvessel density in the mice lung adenoma model. These findings indicate the potential utility of the PRDX4 marker in assessing lung cancer risk.
In stomach cancer cells, PRDX4 regulates EMT through GSDMD-dependent mechanisms. Knockdown of PRDX4 reduces E-cadherin expression, whereas overexpression of PRDX4 increases snail and slug expression. Interestingly, this gene is also involved in cell-to-cell adhesion. By inhibiting gasdermin D, Prdx4 secretion is reduced significantly.
PMID: 9388242 by Jin D.-Y., et al. Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.
PMID: 19892738 by Xu G., et al. Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini.