Recombinant Human Thioredoxin-Dependent Peroxide Reductase, Mitochondrial (PRDX3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-01152P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Thioredoxin-Dependent Peroxide Reductase, Mitochondrial (PRDX3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-01152P
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Product Overview

Description Recombinant Human Thioredoxin-Dependent Peroxide Reductase, Mitochondrial (PRDX3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P30048
Target Symbol PRDX3
Synonyms (Antioxidant protein 1)(AOP-1)(HBC189)(Peroxiredoxin III)(Prx-III)(Peroxiredoxin-3)(Protein MER5 homolog)(Thioredoxin-dependent peroxiredoxin 3)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPANWTPDSPTIKPSPAASKEYFQKVNQ
Expression Range 63-256aa
Protein Length Full Length
Mol. Weight 25.5 kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.
Subcellular Location Mitochondrion. Cytoplasm. Early endosome.
Protein Families Peroxiredoxin family, AhpC/Prx1 subfamily
Database References

HGNC: 9354

OMIM: 604769

KEGG: hsa:10935

STRING: 9606.ENSP00000298510

UniGene: PMID: 28240739

  • 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. PMID: 27958341
  • 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. PMID: 29438714
  • 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. PMID: 27966448
  • The UNG1-PRDX3 interaction protected UNG1 from reactive oxygen species-mediated degradation and prevented mitochondrial DNA oxidation. PMID: 27480846
  • 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 PMID: 26983019
  • 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 PMID: 28045936
  • PRX3 plays a crucial role in mitochondrial homeostasis. PMID: 27037278
  • High PRX3 expression is associated with invasion of lung adenocarcinoma. PMID: 26810067
  • 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 PMID: 26350748
  • Oxidative stress promotes PRX2 and PRX3 hyperoxidation and attenuates pro-survival signaling in aging chondrocytes. PMID: 26797130
  • 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 PMID: 26614766
  • Data indicate that peroxiredoxin III (PrxIII) is a common direct target of both miroRNAs miR-26a-5p and miR-23b-3p. PMID: 24828865
  • 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. PMID: 26091938
  • High serum PRDX3 levels are associated with hepatocellular carcinoma. PMID: 25743848
  • Peroxiredoxin 3 levels regulate a mitochondrial redox setpoint in malignant mesothelioma cells. PMID: 25462069
  • two placental proteins, Prx3 and Prx4, may act as new placental immune targets. PMID: 25323516
  • Serum PRDX3 can be used as a noninvasive biomarker for the diagnosis and/or prognosis of hepatocellular carcinoma. PMID: 24815434
  • High peroxiredoxin 3 protein expression is associated with hepatocellular carcinoma. PMID: 24105047
  • HIF-1alpha is a transcription factor for PRDX3 gene expression in clear cell renal cell carcinoma. PMID: 25093297
  • Data indicate that engineered Prx2 and Prx3 variants C-terminal residues modulate the extent of hyperoxidation. PMID: 24003226
  • The silencing of PRDX3 triggered cisplatinmediated apoptosis in the ovarian cancer cells, which may act through suppression of the NFkappaB signaling pathway. PMID: 23503975
  • Results suggest that PRDX-3 has an essential role in regulating oxidation-induced apoptosis in antiandrogen-resistant prostate cancer cells. PMID: 23880827
  • peroxiredoxin III may be associated with drug resistance in ovarian cancer PMID: 23564483
  • A fraction of FOXM1 coexists in the cytoplasm with mitochondrial peroxiredoxin 3. PMID: 23018647
  • Drug resistance formation was accompanied by a significant increase in the expression of PRDX1, PRDX2, PRDX3, PRDX6 genes in all cancer cell strains, which confirms the importance of redox-dependent mechanisms into development of cisplatin resistance. PMID: 23113308
  • Medulloblastoma tumors exhibit decreased expression of miR-383 but elevated expression of PRDX3. Up-regulation of miR-383 knocks down the expression of PRDX3, inhibits cell proliferation and promotes apoptosis. PMID: 23157748
  • the effects of PRDX3 in PCa progression may be caused by the regulation function of miR-23b, and consequently, miR-23b may be involved in the response of PCa cells to hypoxia stress PMID: 22710126
  • Single nucleotide polymorphisms in the PRDX3 and RPS19 is associated with HPV persistence and cervical precancer/cancer. PMID: 22496757
  • The results indicated that overexpression of PRDX3 was associated with 94.9% hepatocellular carcinoma, and correlated with poor differentiation (P<0.05), which suggest that PRDX3 has substantial clinical impact on the progression of hepatocarcinoma. PMID: 22344546
  • Report nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer. PMID: 22016591
  • Cullin 4B protein ubiquitin ligase targets peroxiredoxin III for degradation. PMID: 21795677
  • The interaction between genetic variations in the PRDX3 gene and dietary fat intake is important for modulation of BMI and obesity risk. PMID: 21127481
  • Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study. PMID: 21385867
  • Paraneoplastic autoimmune reaction against retinal pigment epithelium, with PRDX3 as the putative antigen, may be a cause of acute exudative polymorphous vitelliform maculopathy (AEPVM). PMID: 21220625
  • Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. PMID: 20929858
  • Prx3, which resides within mitochondria, were reacted with a selection of hydroperoxides generated by gamma-radiolysis or singlet oxygen, on free amino acids, peptides and proteins. PMID: 20840079
  • Peroxiredoxin III was significantly up-regulated in cervical cancer tissues. PMID: 20718351
  • Peroxiredoxin III has a significant role in cell cycle regulation and could be a potential proliferation marker in breast cancer. PMID: 20043069
  • Protein levels of Prx-III, a mitochondrial protein were significantly decreased in Alzheimer Disease and Down Syndrome. PMID: 11771746
  • Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site PMID: 11904290
  • PRDX3 is a c-Myc target gene that is requried to maintain normal mitochondrial function. c-Myc directly activates expression of a mitochondrial peroxiredoxin that is required for Myc-mediated transformation. PMID: 12011429
  • LZK was associated directly with the IKK complex through the kinase domain, and that AOP-1 was recruited to the IKK complex through the binding to LZK. PMID: 12492477
  • The level of peroxiredoxin 3 is decreased in the frontal cortex of patients with Down syndrome and Pick's disease. PMID: 12650976
  • Peroxiredoxin III is a critical regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling PMID: 15280382
  • findings indicate that RPK118 is a PRDX3-binding protein that may be involved in transporting PRDX3 from the cytoplasm to its mitochondrial site of function or to other membrane structures via endosome trafficking. PMID: 15750338
  • The additive protection by Trx2 and GSH shows that Trx2 and GSH systems are both functionally important at low oxidative stress conditions. PMID: 17548047
  • Finally, the expression level of beta-globin and GATA-1 was dramatically increased in Prdx III O/E cell line. PMID: 17574212
  • Present throughout lens and localized to mitochondria in lens epithelial cells. Induction is acute response of lens to increased H2O2. Important role in lens H2O2-detoxification, mitochondrial maintenance, and possibly cataract formation. PMID: 17893648
  • FOXO3A mediates Prx III expression, and this may play a critical role in the resistance to oxidative stress in cardiac fibroblasts PMID: 18195003

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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