• Species Reactivity

  Human, Mouse

• Specificity

  Detects human and mouse SOD1/Cu‑Zn SOD in Western blots. Detects rat SOD1, but Catalog #  is recommended. In Western blots, less than 1% cross-reactivity with recombinant human SOD2 or SOD3 is observed.

• Source

  Polyclonal Goat IgG

• Purification

  Antigen Affinity-purified

• Immunogen

  E. coli-derived recombinant human SOD1/Cu‑Zn SOD    
  Met1-Gln154    
  Accession # P00441

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Western Blot

  0.2 µg/mL

  See below

• 
  

• Simple Western

  10 µg/mL

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Reconstitution

  Reconstitute at 0.2 mg/mL in sterile PBS.

• Shipping

  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 Cu  ²⁺ and Zn  ²⁺ 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 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.

• Long Name:

  Superoxide Dismutase-1

• Entrez Gene IDs:

  6647 (Human); 20655 (Mouse); 24786 (Rat)

• Alternate Names:

  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