Recombinant Human PRDX1 Protein (N, C-6His)

Name: Recombinant Human PRDX1 Protein (N, C-6His)
Brand: Beta LifeScience
SKU: BL-1565NP
Availability: InStock

BL-1565NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Peroxiredoxin-1 is produced by our E.coli expression system and the target gene encoding Met1-Lys199 is expressed with a 6His tag at the N-terminus, 6His tag at the C-terminus.
Accession	Q06830
Synonym	Peroxiredoxin-1;Natural killer cell-enhancing factor A;NKEF-A;Proliferation-associated gene protein;PAG;Thioredoxin peroxidase 2;Thioredoxin-dependent peroxide reductase 2;PAGA; PAGB; TDPX2
Gene Background	Peroxiredoxin-1(PRDX1) contains 1 thioredoxin domain and belongs to the AhpC/TSA family. PRDX1 constitutively expressed in most human cells and it is induced to higher levels upon serum stimulation in untransformed and transformed cells. PRDX1 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin and play an important role in eliminating peroxides generated during metabolism. PRDX1 might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. It reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. It may contribute to the antiviral activity of CD8(+) T-cells and have a proliferative effect in cancer development or progression.
Molecular Mass	25.3 KDa
Apmol Mass	26 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of PBS, 10% Glycerol, 0.1mM DTT, pH 6.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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 and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation.
Subcellular Location	Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Families	Peroxiredoxin family, AhpC/Prx1 subfamily
Database References	HGNC: 9352 OMIM: 176763 KEGG: hsa:5052 STRING: 9606.ENSP00000262746 UniGene: Hs.180909

Gene Functions References

Even low doses of radiation employed for dental purposes are capable to provoke stress to cells, which was demonstrated via the induction of the antioxidant gene PRDX1. In elderly patients, such mechanism was demonstrated to be impaired. PMID: 29063384
PRDX1 expression is low in osteosarcoma and fibrosarcoma tumors. PRDX1 suppressed the progression and metastasis of osteosarcoma and fibrosarcoma cells. PMID: 29908016
that Peroxiredoxin1 expression predicted poor prognosis by regulating the tumor metastasis and angiogenesis of colorectal cancer PMID: 29673884
The mRNA and protein levels of Prdx1 in the GC tissues were higher than in the peri-tumor tissues. Authors also found that high Prdx1 expression was positively correlated with the lymph node invasion and poor prognosis. PMID: 29656298
these data ascertain the existence of an H2O2-sensitive PRDX1-FOXO3 signaling axis that fine tunes FOXO3 activity toward the transcription of gene targets in response to oxidative stress. PMID: 28398822
Study uncovered a novel interaction between APE1 and PRDX1, which existed in both the nuclear and cytosolic fractions. Its knockdown enhances APE1 detection in the nucleus and stimulates IL-8 expression. Also, in gastric cancer patients, PRDX1 mRNA expression level is reduced and correlates with poor survival. PMID: 27388124
Median PRDX1 levels were significantly higher in stroke patients compared to controls. PMID: 27924073
The epimutation is present in three generations and results from PRDX1 mutations that force antisense transcription of MMACHC. PMID: 29302025
Peroxiredoxin I (Prx I) increased in tumors of hepatocellular carcinoma (HCC) patients that aligned with overexpression of oncogenic H-ras. PMID: 27517622
Prx1 might play an oncogenic role in tobacco-related oral squamous cell carcinoma and thus serve as a target for chemopreventive and therapeutic interventions. PMID: 27259998
PRDX1 safeguards telomeres from oxygen radicals to counteract telomere damage and preserve telomeric DNA for elongation by telomerase. PMID: 28009281
infection results in S-nitrosylation of multiple host proteins, including Prx1. PMID: 27612662
circulating Prdx1 provides not only prognostic information but may be a promising target against ischemia/reperfusion injury. PMID: 27142532
our findings suggest that the tumor suppressor activity of SIRT2 requires its ability to restrict the antioxidant activity of Prdx-1, thereby sensitizing breast cancer cells to reactive oxygen species -induced DNA damage and cell cytotoxicity PMID: 27503926
UV-vis spectra of heme-PRX1 suggested that Cys52 is the axial ligand of ferric heme. PRX1 peroxidase activity was lost upon heme binding, reflecting the fact that Cys52 is not only the heme-binding site but also the active center of peroxidase activity. PMID: 28082197
Prx1 and Prx2 are likely targets of urate hydroperoxide in cells. Oxidation of Prxs by urate hydroperoxide might affect cell function and be partially responsible for the pro-oxidant and pro-inflammatory effects of uric acid. PMID: 28348082
Data suggest that PRX1 is a dual-function enzyme exhibiting both thioredoxin peroxidase-like activity and catalase-like activity with varied affinities towards reactive oxygen species; studies were conducted using recombinant proteins from green spotted puffer fish Tetraodon nigroviridis and from human. PMID: 28219939
peroxiredoxin 1 has a role in redox sensing and transducing [review] PMID: 27756681
Activation of PRX1 and -2 indicate cold atmospheric plasma affects redox homeostasis in osteosarcoma cells PMID: 28314261
Data show that peroxiredoxins PRDX1 and PRDX2 are upregulated in tumor B cells as compared with normal counterparts. PMID: 26636537
Data show the protein partners of human Prx1 and Prx2 and identified three sequence motifs, or combination thereof in Prxs partners, namely: CXXC, PXXP, and LXXLL. that can be important for protein localization, function and biological pathways. [review] PMID: 26548861
The data indicate that Prdx1 may contribute to the development and progression of hilar cholangiocarcinoma PMID: 26617696
Our data suggest that PRX1 inactivation could represent an interesting strategy to enhance cancer cell sensitivity to vitK3, providing a potential new therapeutic perspective for this old molecule. PMID: 26689287
TRX-1/PRX-1 levels are associated with NADPH oxidase-activity in vivo and in vitro in atherosclerosis. PMID: 26117319
PRDX1 was overexpressed in the tumor tissues of liver cancer and served as an independent poor prognostic factor for overall survival. PRDX1 can be modified by small ubiquitin-like modifier to play specific roles in hepatocarcinogenesis. PMID: 26478675
The immunohistochemistry-based validation using tissue microarray slides in oral squamous cell carcinoma revealed overexpression of the RAB2A and PRDX1 gene in 80 and 68 % of the tested clinical cases, respectively. PMID: 26159854
the protein and mRNA levels of PRDX1 were significantly elevated under insulin-resistant conditions PMID: 26301632
Prdx1 associates with the formation of membrane protrusions through modulation of the activity of p38 MAPK, which in turn promotes pancreatic ductal adenocarcinoma cell invasion. PMID: 25426613
These findings that Prdx1 may be involved in tumorigenesis in esophageal squamous cell carcinoma PMID: 25579166
Dephosphorylation of PrxI by okadaic acid-sensitive phosphatases during late mitosis again shields the centrosome from H2O2 and thereby allows the reactivation of Cdk1-opposing phosphatases at the organelle. PMID: 26150388
This review will summarize the molecular basis of differences in the affinity of Srx for individual Prx and the role of individual component of the Srx-Prx system in tumor progression and metastasis. PMID: 26170166
Overexpression of PRDX1 resulted in a higher resistance of cells to BCNU treatment PMID: 25484280
PRDX1 is shown to be an independent predictor of improved outcomes in ER-positive breast cancer. PMID: 25011585
The K(27)-acetylated hPrx1 exhibited greatly enhanced chaperone activity (e.g. protecting the protein malate dehydrogenase (MDH) from thermally induced aggregation and assisting the refolding of denatured citrate synthase). PMID: 25082442
High level of PRDX1 expression is associated with lymph node metastasis and lung tumor differentiation. PMID: 23914992
MicroRNA-510 promotes cell and tumor growth by targeting peroxiredoxin1 in breast cancer. PMID: 23971998
because of the lower amount of total PRDX1 and PRDX6 and the high thiol oxidation of these PRDXs, very little (less than 20%) protection due to PRDXs remains in infertile men, and this is associated with impaired sperm function and poor DNA integrity PMID: 22492841
Hypoexpression of PRDX1 is associated with papillary thyroid carcinomas. PMID: 24316730
increased Prdx1 expression is associated with tumor angiogenesis and progression in hepatocellular carcinoma PMID: 24297309
results suggest that NGF-trkA signaling is involved in mechanical allodynia in paclitaxel-induced neuropathy PMID: 24480440
The data indicate that Prdx1 may contribute to malignant transformation of the esophagus, and may be used as a biomarker in the immunodiagnosis of ESCC. PMID: 24009050
cellular distribution of Peroxiredoxin I and II in human eyes PMID: 24152995
Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system. PMID: 24062305
Our findings suggest that Prx1 may modulate the chemosensitivity of lung cancer to docetaxel through suppression of FOXO1-induced apoptosis. PMID: 23615915
Prdx1 orchestrates redox signaling in an H2O2 dose-dependent manner through the oxidation status of its peroxidatic cysteine Cys52. PMID: 23334324
Data indicate that AMP-dependent kinases (AMPKalpha1 and AMPKalpha2) inhibit caveolin-1 phosphorylation by stabilizing the interaction between c-Abl and Prdx-1. PMID: 23723070
study identified Pin1 as a novel PRDX1 binding protein and proposed a mechanism for Pin1 in regulating the metabolism of reactive oxygen species in cells PMID: 23421996
expression of Prxs I and IV, both at mRNA and protein levels, was associated with light chain secretion quantified by ELISA. PMID: 23737084
observations suggest that PRDX1 acts as a pro-cancer protein in HCC HepG2 cells. PMID: 23277276
The protein and mRNA expressions of Prx1 and Prx6 increased significantly in the order of normal brain tissue, grade II astrocytoma, grade III astrocytoma and grade IV astrocytoma. PMID: 22985558

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