Anti-Peroxiredoxin 1

Replaces: 07-609

Concentration: Please refer to lot specific datasheet.

Affinity Purified

Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Evaluated by Western Blotting in DU145 cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Peroxiredoxin 1 in 10 µg of DU145 cell lysate.

Anti-Peroxiredoxin 1 Antibody, Cat. No. 07-609-I, is a highly specific rabbit polyclonal antibody that targets Peroxiredoxin 1 and has been tested in Immunocytochemistry, Immunohistochemistry (Paraffin) and Western Blotting.

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected Peroxiredoxin 1 in HeLa cells.

Immunohistochemistry Analysis: A 1:250-1:1,000 dilution from a representative lot detected Peroxiredoxin 1 in human kidney, human small intestine, and human cerebellum tissues.

Research Category
Neuroscience

Predicted to react with various other mammalian species, including Bat, Canine, Hamster, Rat, and Rhesus Monkey.

This polyclonal antibody detects Peroxiredoxin-1 by Western blotting and immunocytochemistry in in DU145 cells and HeLa cells, respectively.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Peroxiredoxin-1 (UniProt: Q06830; also known as EC:1.11.1.15, Natural killer cell-enhancing factor A, NKEF-A, Proliferation-associated gene protein, PAG, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2) is encoded by the PRDX1 (also known as PAGA, PAGB, TDPX2) gene (Gene ID: 5052 ) in human. Peroxiredoxins belong to a family of non-seleno peroxidases. Thus far six different mammalian isoforms have been reported and they all catalyze peroxide reduction of hydrogen peroxide, organic hydroperoxides and peroxynitrite. All peroxiredoxins share a conserved Cys residue that corresponds to the N-terminal Cys51 in mammalian peroxiredoxin-1. Peroxiredoxin 1-4 also contain an additional conserved Cys residue in the C-terminal region, Cys172. The N-terminal Cys51 is shown to be oxidized by hydrogen peroxide to form cysteine-sulfenic acid (Cys51-SOH) and reacts with Cys172-SH of the other subunit to produce an intermolecular disulfide, which can only be reduced by thioredoxin and not by glutathione or glutaredoxin. Peroxiredoxin-1 is constitutively expressed in most human cells and is induced to higher levels upon serum stimulation in cells. It is involved in redox regulation of the cell and important role in overcoming oxidative stress. Peroxiredoxin-1 also eliminates peroxides generated during drug metabolism. It is phosphorylated on Thr90 during the M-phase of cell cycle, which leads to over 80% reduction in its enzymatic activity.

~21 kDa observed; 22.11 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

KLH-conjugated linnear peptide corresponding to 12 amino acids from the C-terminal region of human Peroxiredoxin-1.

Stable for 1 year at 2-8°C from date of receipt.