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: All products, High-quality recombinant proteins, Other 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: 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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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.

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