PRDX1 Human

Peroxiredoxin-1 Human Recombinant
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Description

Overview of PRDX1

PRDX1 belongs to the peroxiredoxin family, which detoxifies reactive oxygen species (ROS) such as hydrogen peroxide (H2O2H_2O_2) and organic hydroperoxides . It maintains redox homeostasis by regulating H2O2H_2O_2 levels, which are essential for signaling pathways controlling cell growth, differentiation, and apoptosis . PRDX1 also exhibits non-canonical roles in epigenetic regulation and tumorigenesis .

Key Features:

  • Gene Location: Chromosome 1 (1p34.1), adjacent to MMACHC .

  • Protein Structure: Thioredoxin-dependent peroxidase with conserved catalytic cysteine residues .

  • Mechanism: Reduces H2O2H_2O_2 to water, preventing oxidative damage .

Tissue Expression:

PRDX1 is ubiquitously expressed, with high levels in the liver, lung, and kidney . Its subcellular localization includes the cytoplasm, nucleus, and mitochondria .

Methylmalonic Acidemia with Homocystinuria (epi-cblC):

PRDX1 variants cause promoter hypermethylation of the nearby MMACHC gene, disrupting vitamin B12 metabolism . This leads to:

  • Developmental delays

  • Neurological abnormalities

  • Hematologic defects .

Genetic MechanismClinical OutcomeReferences
PRDX1 variants → MMACHC hypermethylationReduced MMACHC protein → Impaired B12 processing

Dual Role in Cancer

PRDX1 exhibits context-dependent roles in cancer, acting as both a tumor suppressor and promoter .

Tumor Suppressor Functions:

  • Breast Cancer: Inhibits ROS-mediated estrogen receptor α degradation; associated with favorable prognosis .

  • Lung Cancer: Modulates K-Ras/ERK signaling to suppress tumor growth .

Tumor Promoter Functions:

  • Osteosarcoma: Overexpression enhances metastasis via Akt/mTOR pathway activation .

  • Prostate Cancer: Stabilizes androgen receptor signaling, promoting proliferation .

Cancer TypeRole of PRDX1MechanismReferences
OsteosarcomaPromotes metastasisActivates Akt/mTOR; enhances cell migration
Breast CancerSuppresses tumor growthReduces oxidative stress; inhibits ERα loss
Esophageal Squamous Cell CarcinomaDrives tumorigenesisActivates mTOR/p70S6K pathway

Targeting PRDX1:

  • Inhibition: Adenanthin (a PRDX1 inhibitor) sensitizes breast cancer cells to prooxidant therapies .

  • CAR NK Cells: PRDX1-overexpressing NK cells show enhanced antitumor activity under oxidative stress .

Product Specs

Introduction
PRDX1, a member of the peroxiredoxin family of antioxidant enzymes, plays a crucial role in reducing hydrogen peroxide and alkyl hydroperoxides. This enzyme is vital for protecting red blood cells from reactive oxygen species and preventing tumor formation. PRDX1 exhibits antioxidant properties within cells, contributing to the antiviral activity of CD8(+) T-cells. Additionally, it demonstrates a proliferative effect and is implicated in cancer development and progression. Functioning as a key player in cellular redox regulation, PRDX1 reduces peroxides using reducing equivalents supplied by the thioredoxin system, not glutaredoxin. This enzyme is essential for eliminating peroxides generated during metabolism and participates in the signaling pathways of growth factors and TNF-alpha by controlling intracellular h(2)o(2) concentrations.
Description
Recombinant Human Peroxiredoxin, fused with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain (1-199) consists of 219 amino acids and has a molecular weight of 24 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The Peroxiredoxin solution is provided at a concentration of 1mg/ml in a buffer containing 20mM Tris-HCl (pH 7.5) and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain product integrity, avoid repeated freeze-thaw cycles.
Purity
The purity of the Peroxiredoxin is determined to be greater than 90% using SDS-PAGE analysis.
Biological Activity
Enzymatic activity is determined by measuring the amount of hydroperoxide reduced by 1ug of enzyme per minute at 25°C. The specific activity of this Peroxiredoxin is greater than 2,000 pmol/min/ug.
Synonyms
Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK.

Q&A

Basic Research Questions

  • What is the PRDX1 gene and what function does the encoded protein serve?

    The PRDX1 gene provides instructions for synthesizing peroxiredoxin-1 protein, which belongs to the peroxiredoxin family of proteins. These proteins primarily protect cells from damage caused by reactive oxygen species (ROS). PRDX1 specifically breaks down hydrogen peroxide, which at low levels participates in chemical signaling pathways controlling cellular functions like growth, maturation, and survival. By regulating hydrogen peroxide levels, PRDX1 helps control these signaling pathways while protecting cells from the toxic effects of high hydrogen peroxide concentrations, which can damage DNA, proteins, and cell membranes .

  • What experimental methods are commonly used to detect PRDX1 expression in tissue samples?

    Several complementary techniques are employed for comprehensive PRDX1 detection:

    • qRT-PCR: For measuring PRDX1 mRNA levels in fresh tumor and perihematomal tissues

    • Western blotting: For analyzing PRDX1 protein levels in tissue samples

    • Immunohistochemistry (IHC): For visualizing PRDX1 expression in tissue sections and quantifying PRDX1-positive cells

    • Immunofluorescence staining: For investigating cellular localization of PRDX1 and co-localization with cell-specific markers (e.g., GFAP for astrocytes, Iba1 for microglia)

    • RNA-seq and RIP-seq: For advanced studies of gene expression patterns and RNA interactions

  • What is the temporal expression profile of PRDX1 in pathological conditions?

    In rat models of intracerebral hemorrhage (ICH), PRDX1 shows a distinct temporal expression pattern. PRDX1 mRNA levels increase at 24 hours post-ICH, peak at 72 hours, and then gradually decline. Protein levels show significant elevation at 3 days post-ICH compared to control groups. Notably, this peak expression at 72 hours coincides with statistically significant differences in mortality between experimental groups, suggesting a critical role for PRDX1 in the subacute phase of ICH-induced brain injury .

  • Which pathologies are associated with PRDX1 alterations?

    PRDX1 has been implicated in several pathological conditions:

    • Methylmalonic acidemia with homocystinuria, epi-cblC type: Variants in the PRDX1 gene can cause promoter hypermethylation of the nearby MMACHC gene, leading to developmental delay, eye defects, neurological problems, and blood abnormalities .

    • Osteosarcoma: Overexpression of PRDX1 is frequently observed in osteosarcoma tissues and cell lines, correlating with tumor size, high malignant grade, and advanced TNM stage .

    • Intracerebral hemorrhage: PRDX1 plays a neuroprotective role by targeting inflammation and apoptosis-related mRNA stability, reducing ICH-induced brain injury .

  • How can researchers analyze the correlation between PRDX1 expression and clinical parameters?

    A methodological approach includes:

    • Establishing training and validation cohorts from different centers to ensure reproducibility

    • Using independent t-tests for evaluating differences between samples and ANOVA for multiple group comparisons

    • Applying Kaplan-Meier survival curves and log-rank tests to compare survival between groups with different PRDX1 expression levels

    • Performing univariate and multivariate analyses to determine if PRDX1 is an independent predictor of survival by calculating hazard ratios (HR) and confidence intervals (CI)

    • Using standardized scoring systems for immunohistochemical evaluation of PRDX1 expression

Product Science Overview

Structure and Function

PRDX1 is a thiol peroxidase that catalyzes the reduction of peroxides, including hydrogen peroxide. It functions similarly to other antioxidant enzymes like catalase and glutathione peroxidase . PRDX1 is part of the 2-Cys peroxiredoxin subfamily, which requires the oxidation of two cysteine residues to activate its enzymatic activity . The enzyme is abundant in the cytosol of mammalian cells and plays a significant role in maintaining intracellular reactive oxygen species (ROS) homeostasis .

Biological Roles
  1. Antioxidant Protection: PRDX1 helps in detoxifying peroxides, thus protecting cells from oxidative stress .
  2. Antiviral Activity: It may contribute to the antiviral activity of CD8 (+) T-cells .
  3. Tumor Suppression: PRDX1 has been shown to play roles in tumor suppression and apoptosis .
  4. Molecular Chaperoning: It also functions as a molecular chaperone, assisting in the proper folding of proteins .
Clinical Significance

PRDX1 is essential for the viability and maintenance of ROS levels in cells. Studies have shown that depletion of PRDX1 results in increased intracellular ROS levels and cell death . PRDX1 knockout mice have been observed to develop severe hemolytic anemia and several malignant cancers, indicating its role in preventing tumor development .

Recombinant PRDX1

Recombinant human PRDX1 is produced using an Escherichia coli expression system. It is used in various research applications, including functional studies and SDS-PAGE . The recombinant protein is stored at -20°C and is typically provided in a buffer containing 20 mM Hepes, pH 7.0, with 10% glycerol and 1 mM DTT .

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