Detection of Human/Mouse/Rat Peroxiredoxin 1 by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line, Raji human Burkitt's lymphoma cell line,|
MCF‑7 human breast cancer cell line, CH-1 mouse B cell lymphoma cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human/Mouse/Rat Peroxiredoxin 1 Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF3488) followed by HRP‑conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for Peroxiredoxin 1 at approximately 22 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 2.
Detection of Human Peroxiredoxin 1 by Simple WesternTM. Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line and Raji human Burkitt's lymphoma cell line, loaded at 0.2 mg/mL. A specific band was detected for Peroxiredoxin 1 at approximately 29 kDa (as indicated) using 2 µg/mL of Goat Anti-Human/Mouse/Rat Peroxiredoxin 1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3488) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
Human Peroxiredoxin 1 (Prx-1 or PRDX1; also 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. Inactive, it 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 shows 96% and 98% amino acid identity to mouse and rat Prx-1, respectively.
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