Human/Mouse/Rat Peroxiredoxin 2 Alexa Fluor® 405-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Peroxiredoxin 2

Human peroxiredoxin-2 (Prx-2 or PRDX2; also Thioredoxin Peroxidase 1) is a 22 kDa antioxidant enzyme that belongs to the typical 2-Cys class of the THP/ahpC family of proteins. The precursor molecule is 198 amino acids (aa) in length, and has two catalytic cysteines, one at Cys50 and a second at Cys171. Prx-2 is an obligate homodimer. Inactive, it is apparently noncovalently associated. Upon peroxide binding to Cys50 of subunit 1, the Cys171 of subunit 2 interacts with Cys50 of subunit 1 to complete the antioxidation, generating a disulfide bond between Cys50 and Cys171. Subsequent reduction restores the subunits to the basal state. There are two additional isoforms. Isoform-b shows a deletion of aa 36‑86, while isoform c shows a substitution of 56 aa after residue 86. Human Prx-2 is 93% aa identical to mouse and rat Prx-2.

Product Datasheets

Related Research Areas

• Anti-oxidant Molecules
• Cancer Biomarkers
• Oxidative Stress