PRDX5 Human

Peroxiredoxin-5 Human Recombinant
Cat. No.
BT25246
Source
Escherichia Coli.
Synonyms
Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PRDX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (53-214 a.a.) and having a molecular mass of 17 kDa.
The PRDX5 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PRDX5, a member of the peroxiredoxin family, is an antioxidant enzyme that plays a crucial role in reducing hydrogen peroxide and alkyl hydroperoxides. This process utilizes reducing equivalents provided by the thioredoxin system. Found in various tissues, PRDX5 provides antioxidant protection under normal physiological conditions and during inflammatory responses. Notably, it interacts with peroxisome receptor 1 and participates in intracellular redox signaling. PRDX5 is particularly important in lung epithelial cells, where its expression increases during inflammation, highlighting its role as a significant antioxidant protein in the lungs. Moreover, PRDX5 expression is elevated in osteoarthritis and potentially contributes to mitochondrial genome stability. In human tendon cells, it exerts a protective effect against oxidative stress by reducing apoptosis and supporting collagen synthesis.
Description
Recombinant human PRDX5, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 162 amino acids (spanning positions 53 to 214) and has a molecular weight of 17 kDa. The purification of PRDX5 is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterile filtered.
Formulation
The PRDX5 solution is supplied in 20mM HEPES buffer with a pH of 7.4.
Stability

For optimal storage, refrigerate the vial at 4°C if the entire contents will be used within 2-4 weeks. For extended storage periods, freeze the product at -20°C. Adding a carrier protein, such as 0.1% HSA or BSA, is recommended for long-term storage. Avoid repeated freeze-thaw cycles to maintain product integrity.

Purity
SDS-PAGE analysis indicates a purity greater than 95.0%.
Biological Activity
The specific activity of PRDX5 has been determined to be approximately 117-136 picomoles per minute per microgram (pmole/min/µg). This enzymatic activity was measured by quantifying the remaining peroxide after incubating PRDX5 with peroxide for 20 minutes at room temperature. Specific activity refers to the amount of hydroperoxide reduced by 1 microgram of enzyme at 25°C within 1 minute.
Synonyms
Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.
Source
Escherichia Coli.
Amino Acid Sequence
MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA EALKAKGVQV VACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPNIIS QL.

Product Science Overview

Introduction

Peroxiredoxin-5 (PRDX5) is a member of the peroxiredoxin family of antioxidant enzymes. These enzymes play a crucial role in reducing hydrogen peroxide and alkyl hydroperoxides, thereby protecting cells from oxidative damage. PRDX5 is encoded by the PRDX5 gene located on chromosome 11 in humans .

Structure and Localization

PRDX5 is unique among the peroxiredoxin family due to its large subcellular distribution. It can be localized to mitochondria, peroxisomes, the cytosol, and the nucleus . The protein structure of PRDX5 includes an N-terminal domain and a unique alpha helix that replaces a loop structure found in typical thioredoxin domains . Unlike other peroxiredoxins that form anti-parallel dimers, PRDX5 forms dimers through close contact between specific alpha helices .

Function

PRDX5 functions as a thiol-specific peroxidase, catalyzing the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively . This activity is essential for cell protection against oxidative stress. PRDX5 also acts as a sensor for hydrogen peroxide-mediated signaling events . Overexpression of PRDX5 has been shown to inhibit peroxide accumulation and reduce cell death induced by oxidative stress .

Expression and Regulation

PRDX5 is widely expressed in various tissues and its expression can be upregulated during inflammatory processes . For instance, PRDX5 expression increases in lung epithelial cells during inflammation and is also upregulated in conditions such as osteoarthritis .

Clinical Significance

The antioxidative and cytoprotective functions of PRDX5 make it a significant protein in maintaining cellular health. Reduced expression of PRDX5 can lead to increased susceptibility to oxidative damage and apoptosis . Additionally, PRDX5 has been shown to promote longevity in model organisms like Drosophila melanogaster .

Recombinant PRDX5

Human recombinant PRDX5 is produced using recombinant DNA technology, which allows for the expression of the PRDX5 protein in various host systems. This recombinant form is used in research to study the protein’s function, structure, and potential therapeutic applications.

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