Detection of Mouse/Rat SOD1/Cu-Zn SOD by Western Blot.
Western blot shows lysates of NIH-3T3 mouse embryonic fibroblast cell line and NRK rat normal kidney cell line. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Mouse/Rat SOD1/Cu-Zn SOD Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3787) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for SOD1/Cu-Zn SOD at approximately 19 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 2.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
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 converversion 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 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. Mouse SOD1 is 97% aa identcal to rat SOD1. Mutations in SOD1 have been suggested to be the cause 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 mutations in SOD1 result in the intracellular accumulation of the 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.
Submit a review and receive a $25US/€18/£15/$25CAN amazon gift card if you include an image - $10US/€7/£6/$10CAN Amazon card for reviews without an image. Limited to verified customers in USA, Canada and Europe.