| Reactivity | Hu, Mu, RtSpecies Glossary |
| Applications | WB, KO |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | Alexa Fluor 532 |
| Immunogen | E. coli-derived recombinant human Peroxiredoxin 1 Met1-Lys199 Accession # Q06830 |
| Specificity | Detects human, mouse and rat Peroxiredoxin 1 in Western blots. In direct ELISAs, less than 1% cross‑reactivity with recombinant human Peroxiredoxin 3 or 4 is observed. |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Purity Statement | Antigen Affinity-purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
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.
Secondary Antibodies |
Isotype Controls |
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