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Antibody is stable for 24 months.
Positive Control: HepG2, HeLa and Jurkat cell lysates. Ovarian carcinoma tissue. Cellular Localization: Cytoplasm. Secreted.
Specificity Comments: The peroxiredoxin (PRX) family comprises six antioxidant proteins, PRX I, II, III, IV, V and VI, which protect cells from reactive oxygen species (ROS) by preventing the metal-catalyzed oxidation of enzymes. The PRX proteins primarily utilize thioredoxin as the electron donor for antioxidation, although they are fairly promiscuous with regard to the hydroperoxide substrate. In addition to protection from ROS, peroxiredoxins are also involved in cell proliferation, differentiation and gene expression. PRX I, II, IV and VI show diffuse cytoplasmic localization, while PRX III and V exhibit distinct mitochondrial localization. The human PRX IV gene is expressed in many tissues. It exists as a precursor protein, which is only detected in testis, and aprocessed secreted form. PRX IV is highly expressed in lung cancer and is necessary for the promotion of lung cancer in vitro. Studies have demonstrated that PRX IV positive expression is significantly correlated with recurrences and shorter disease-free survival in patients with early-stage lung squamous cell carcinoma, and therefore can be used as a prognostic marker in lung squamous cell carcinoma.
Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20-30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Antioxidant enzyme AOE372; AOE37-2; EC 1.11.1.15; epididymis secretory sperm binding protein Li 97n; Peroxiredoxin IV; Peroxiredoxin-4; Prx 4; Prx-IV; Thioredoxin dependent peroxide reductase A0372; thioredoxin peroxidase (antioxidant enzyme); Thioredoxin peroxidase AO372; Thioredoxin-dependent peroxide reductase A0372; Thioredoxin-dependent peroxiredoxin 4
Gene Aliases: AOE37-2; AOE372; HEL-S-97n; PRDX4; PRX-4
UniProt ID: (Human) Q13162
Entrez Gene ID: (Human) 10549
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