Thioredoxin reductase

Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the β-oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to a great extent suggesting that they has a proliferative effect and may be related to cancer development or progression. Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase that belongs to the atypical 2-Cys class of the TSA ahpC family of peroxiredoxins. PRDX5 is a widely expressed mitochondrial antioxidant enzyme that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. In human cells, this enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus.

Expression system: E. coli
Length: 37-524 (mutation), Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 63-256, Partial
Activity: Not Tested

PRDX1 Protein, Human, Recombinant (His) is expressed in E. coli. The accession number is Q06830.

Expression system: E. coli
Length: 63-256, Partial
Activity: Not Tested

Peroxiredoxin-4 (PRDX4) is a member of the AhpC TSA family. PRDX4 is a cytoplasmic protein and contains one thioredoxin domain. PRDX4 exists in homodimer or heterodimer with PRDX1. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. In addition, PRDX4 is probably involved in redox regulation of the cell, regulating the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

Expression system: E. coli
Length: 60-166, Full Length
Activity: Enzyme activity

Expression system: E. coli
Length: 161-647, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-123, Full Length
Activity: Not Tested