| Field | Specification |
|---|---|
| Accession Number | |
| Alternative Names | Superoxide dismutase [Cu-Zn], Cu/Zn superoxide dismutase, SOD1, ALS1, SODC_HUMAN, Superoxide dismutase1, IPOA, SODC |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Synthetic Rat Cu/Zn SOD Peptide |
| Product Type | |
| Reactivity | |
| Shipping | |
| Storage | |
| Target |
Superoxide dismutase 1 (SOD1) is a copper- and zinc-dependent antioxidant enzyme that plays a vital role in cellular defense against oxidative stress. Present in nearly all mammalian cells, SOD1 catalyzes the dismutation of superoxide radicals (O₂⁻) into hydrogen peroxide (H₂O₂) and molecular oxygen (O₂). These reactive oxygen species are subsequently detoxified by catalase and glutathione peroxidase, maintaining redox balance and protecting cells from oxidative damage.
SOD1 functions as a 32 kDa homodimer, with each 16 kDa subunit stabilized by an intra-subunit disulfide bridge and a conserved β-barrel structure. It is primarily localized in the cytoplasm but also found in the nucleus and mitochondrial intermembrane space. Its structural integrity and metal-binding capacity are essential for enzymatic activity and cellular protection.
In neuroscience and neurodegenerative disease research, SOD1 has gained prominence due to its association with amyotrophic lateral sclerosis (ALS). Mutations in the SOD1 gene can lead to protein misfolding, aggregation, and toxic gain-of-function effects, contributing to motor neuron degeneration. These pathological forms of SOD1 are key biomarkers and therapeutic targets in ALS and related disorders.
Understanding the structure-function relationship of SOD1, particularly its metal coordination and dimerization, is critical for developing targeted interventions in oxidative stress-related neurodegeneration.
0.5 µg/ml of SPC-115 was sufficient for detection of Cu/Zn SOD in 20 µg of rat brain tissue extract by colorimetric immunoblot analysis using Goat anti-rabbit IgG:AP as the secondary antibody.
Cite this product varies by variant:
- SPC-115D — Size: 100 ug: SOD1 (Cu/Zn) Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D, RRID: AB_2193769)
- SPC-115D-A390 — Size: 100 ug: SOD1 (Cu/Zn) Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-A390, RRID: AB_2703347)
- SPC-115D-A488 — Size: 100 ug: SOD1 (Cu/Zn) Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-A488, RRID: AB_2703348)
- SPC-115D-A594 — Size: 100 ug: SOD1 (Cu/Zn) Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-A594, RRID: AB_2703350)
- SPC-115D-APC — Size: 100 ug: SOD1 (Cu/Zn) Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-APC, RRID: AB_2703356)
- SPC-115D-BI — Size: 100 ug: SOD1 (Cu/Zn) Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-BI, RRID: AB_2703357)
- SPC-115D-FITC — Size: 100 ug: SOD1 (Cu/Zn) Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-FITC, RRID: AB_2703358)
- SPC-115D-HRP — Size: 100 ug: SOD1 (Cu/Zn) Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-HRP, RRID: AB_2703359)
- SPC-115D-PCP — Size: 100 ug: SOD1 (Cu/Zn) Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-PCP, RRID: AB_2703361)
- SPC-115D-RPE — Size: 100 ug: SOD1 (Cu/Zn) Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115D-RPE, RRID: AB_2703362)
- SPC-115S — Size: 12 ug: SOD1 (Cu/Zn) Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-115S, RRID: AB_2193769)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
2. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180.
3. Furukawa Y., O'Halloran T. (2006). Antioxidants & Redo Signaling. Vol 8, No 5,6.
4. Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol 284: L917-L925.
5. Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385.
6. Kurobe N., et al. (1990) Biomedical Research. 11: 187-194
7. Wispe J.R., et al. (1989) BBA. 994: 30-36.
8. Xiao-Hong Liu., et al. (1993) Brain Research. 625: 29-37.
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