Human SOD1/Cu-Zn SOD Alexa Fluor® 750-conjugated Antibody

Applications

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.

Preparation and Storage

Background: SOD1/Cu-Zn SOD

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.

Product Datasheets

Related Research Areas

• ALS Related Molecules
• Anti-oxidant Molecules
• DNA Damage and Repair
• Microglia Activation
• ROS and Stress Resistance