SOD1/Cu-Zn SOD Antibody [Alexa Fluor® 532]

• Reactivity: Mu, Rt
• Applications: WB
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Alexa Fluor 532

SOD1/Cu-Zn SOD Antibody [Alexa Fluor® 532] Summary

• Immunogen: E. coli-derived recombinant mouse SOD1
  Met1-Gln154
  Accession # P08228
• Specificity: Detects endogenous mouse and rat SOD1 in Western blots. In Western blots, this antibody shows no cross‑reacivity with recombinant human SOD2 or SOD3.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Western Blot

Packaging, Storage & Formulations

• 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

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for SOD1/Cu-Zn SOD Antibody [Alexa Fluor® 532]

• ALS
• ALS1
• amyotrophic lateral sclerosis 1 (adult)
• Cu
• Cu/Zn superoxide dismutase
• CuZn SOD
• Cu-Zn SOD
• EC 1.15.1.1
• homodimer
• hSod1
• indophenoloxidase A
• Ipo1
• IPOA
• SOD
• SOD, cytosolic
• SOD, Soluble
• SOD1
• superoxide dismutase [Cu-Zn]
• Superoxide dismutase 1
• superoxide dismutase 1, soluble
• Zn superoxide dismutase, EC 1.15.1.110superoxide dismutase, cystolic

Background

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. 

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.