LifeTein - Superoxide Dismutase

Superoxide dismutase is a metalloenzyme. It is present in all living organisms, including animals, plants, and microorganisms. SOD is categorized based on its metallicity into copper, zinc-SOD (Cu, Zn-SOD), manganese-SOD (Mn-SOD), and iron-SOD (Fe-SOD). LifeTein`s recombinant Superoxide Dismutase belongs to Human Copper, Zinc-Superoxide Dismutase (rh-SOD1).

LifeTein`s Superoxide Dismutase1 (SOD1) is expressed and purified from E.coli. The N terminal sequence is ATKAVCVLKG. This enzyme binds to molecules of copper and zinc to break down toxic, charged oxygen molecules called superoxide radicals. The physiological significance of SOD is that it can convert toxic superoxide free radicals into hydrogen peroxide.

Superoxide radicals can damage cells if too many accumulate within cells. Superoxide radicals are byproducts of normal cell processes, particularly energy-producing reactions, and must be broken down regularly. It is living organisms’ primary means of scavenging oxygen free radicals.

Almost 60 diseases have been shown to be directly related to oxygen free radicals and the level of SOD has used as an indicator of aging and death. SOD has recently gained notoriety for its connection with amyotrophic lateral sclerosis (ALS), more commonly known as Lou Gehrig`s disease, a condition characterized by progressive movement problems and muscle wasting. This disease is a degenerative disorder that leads to selective death of neurons in the brain and spinal cord, leading to gradually increasing paralysis. At least 170 mutations in the SOD1 gene have been found to cause ALS. Most of these mutations change one of the amino acids in the superoxide dismutase enzyme. About half of all Americans with ALS caused by SOD1 gene mutations have a particular mutation that replaces the amino acid alanine with the amino acid valine at position 4 in the enzyme.