Human Peroxiredoxin 1 Alexa Fluor® 350-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 1

Human Peroxiredoxin1 (Prx-1, also known as Thioredoxin peroxidase 2) is a 22 kDa antioxidant enzyme that belongs to the typical 2-Cys class of the THP/ahpC family of proteins. The molecule is 199 amino acids (aa) in length and has two catalytic cysteines, one at Cys52 and a second at Cys173. Prx-1 is an obligate homodimer. In its inactive state, Prx-1 is apparently noncovalently associated. Upon peroxide binding to Cys52 of subunit 1, the Cys173 of subunit 2 interacts with Cys52 of subunit 1 to complete the antioxidation, generating a disulfide bond between Cys52 and Cys173. Subsequent reduction restores the subunits to the basal state. There are apparently two additional isoforms; one shows a premature truncation after aa 171, while the second shows a deletion of aa 21‑121. Human Prx-1 is 96% aa identical to mouse Prx-1.

Product Datasheets

Related Research Areas

• Anti-oxidant Molecules
• Natural Killer T (NKT) Cells
• Oxidative Stress