SOD1/Cu-Zn SOD Antibody (348808) [Alexa Fluor® 350]

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Product Details

Summary
Applications WB, ICC/IF, KO
Clone
348808
Clonality
Monoclonal
Host
Mouse
Conjugate
Alexa Fluor 350

Order Details

SOD1/Cu-Zn SOD Antibody (348808) [Alexa Fluor® 350] Summary

Immunogen
E. coli-derived recombinant human SOD1/Cu‑Zn SOD
Met1-Gln154
Accession # P00441
Specificity
Detects human SOD1/Cu‑Zn SOD in Western blots. In Western blots, no cross-reactivity with recombinant human (rh) SOD2 or rhSOD3 is observed.
Isotype
IgG2a
Clonality
Monoclonal
Host
Mouse
Purity Statement
Protein A or G purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

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.

Background

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.

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.

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