Mouse/Rat SOD1/Cu-Zn SOD Alexa Fluor® 700-conjugated Antibody

Catalog # Availability Size / Price Qty
AF3787N-100UG

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Mouse/Rat SOD1/Cu-Zn SOD Alexa Fluor® 700-conjugated Antibody Summary

Species Reactivity
Mouse, Rat
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.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
E. coli-derived recombinant mouse SOD1
Met1-Gln154
Accession # P08228
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Label
Alexa Fluor 700 (Excitation= 675-700 nm, Emission= 723 nm)

Applications

Recommended Concentration
Sample
Western Blot
Optimal dilution of this antibody should be experimentally determined.
 

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

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Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

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. 

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

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