Detection of Human SOD1/ Cu‑Zn SOD by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line and Ramos human Burkitt's lymphoma cell line. PVDF membrane was probed with 0.5 µg/mL Mouse Anti-Human SOD1/Cu‑Zn SOD Monoclonal Antibody (Catalog # MAB3418) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). For additional reference, recombinant human SOD1, SOD2, and SOD3 (1 ng) were included. A specific band for SOD1/Cu-Zn SOD was detected at approximately 16 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.
SOD1/Cu‑Zn SOD in HeLa Human Cell Line. SOD1/Cu‑Zn SOD was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Mouse Anti-Human SOD1/Cu‑Zn SOD Monoclonal Antibody (Catalog # MAB3418) at 25 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: SOD1/Cu-Zn SOD
Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 1, SOD1, also known as Cu/Zn SOD, soluble SOD and IPO-A, is a soluble, cytoplasmic 16 kDa homodimer. Each SOD1 monomer binds one Cu2+ and one Zn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD1 shares 23% and 27% sequence identity with SOD2 and SOD3, respectively. Mutations in SOD1 have been implicated as causes of familial amyotrophic lateral sclerosis (ALS). The ALS-causing mutations of SOD1 are scattered throughout the protein and provide no clear functional or structural clues to the underlying disease mechanism. The oligomerization hypothesis suggests that mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight aggregates that result in the death of motor neurons. The oxidative damage hypothesis suggests that loss of function mutation in SOD1 protein results in the accumulation of cellular superoxide radical, leading to free radical-mediated damage, the release of cytochrome c, and apoptosis.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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