| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
SOD2, also known as manganese superoxide dismutase, serves as a critical mitochondrial enzyme that catalyzes the dismutation of superoxide radicals into hydrogen peroxide and oxygen. This antioxidant defense mechanism plays a fundamental role in protecting cells from oxidative stress, making SOD2 a key target in research spanning cancer biology, neurodegeneration, cardiovascular disease, and metabolic disorders. Dysregulation of SOD2 expression has been implicated in tumor progression, aging, and inflammatory conditions, underscoring its importance across multiple disease contexts.
This recombinant monoclonal antibody, generated from clone 10F6 in rabbit host, offers the reproducibility and consistency that demanding experimental workflows require. Because recombinant antibodies are produced from defined sequences rather than traditional hybridoma methods, researchers benefit from lot-to-lot uniformity that supports reliable longitudinal studies and reproducible results across laboratories.
Validation testing demonstrates robust performance across multiple applications. In Western blot analysis, the antibody detects a clear band at the expected 25 kDa molecular weight across diverse human cell lines including HeLa, MCF-7, HepG2, U87, and K562, as well as rat brain tissue and additional brain and liver tissue samples. This cross-species reactivity between human and rat samples provides flexibility for researchers working with different model systems. For immunohistochemistry, the antibody has been validated in paraffin-embedded human liver cancer tissue, producing specific staining that enables visualization of SOD2 expression patterns in clinical specimens.
Whether investigating mitochondrial dysfunction in neurodegenerative models, examining oxidative stress responses in cancer cells, or exploring metabolic signaling pathways, this antibody provides a dependable tool for advancing your research objectives.
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