SOD1 Human
Greater than 95.0% as determined by SDS-PAGE.
Description
The SOD1 is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Superoxide Dismutase 1 (SOD1) is a crucial enzyme in the human body, responsible for protecting cells from oxidative damage by catalyzing the dismutation of superoxide radicals into oxygen and hydrogen peroxide . This enzyme is encoded by the SOD1 gene located on chromosome 21 . Recombinant human SOD1 is produced using various expression systems, such as Escherichia coli and Bacillus subtilis, to meet the demand for research and therapeutic applications .
SOD1 is a homodimeric enzyme, with each subunit containing 154 amino acids and a molecular mass of approximately 32 kDa . The enzyme’s active site binds copper and zinc ions, which are essential for its catalytic activity . The primary function of SOD1 is to convert superoxide radicals, which are harmful byproducts of aerobic metabolism, into less reactive molecular oxygen and hydrogen peroxide . This process is vital for maintaining cellular homeostasis and preventing oxidative stress-induced damage to DNA, proteins, and lipids .
Recombinant human SOD1 is typically expressed in E. coli or Bacillus subtilis . The expression conditions, such as inoculum size, media composition, temperature, and inducer concentration, are optimized to achieve high yields of soluble and biologically active enzyme . For instance, in Bacillus subtilis, the highest level of hSOD1 production was achieved using a 2% inoculum with 0.2 mM IPTG at 37°C for 24 hours . The enzyme is then purified using chromatographic methods to obtain a high-purity product suitable for research and therapeutic applications .
SOD1 plays a pivotal role in the antioxidant defense system, making it a valuable therapeutic agent for various diseases associated with oxidative stress, such as amyotrophic lateral sclerosis (ALS), Parkinson’s disease, and acute inflammation . Recombinant human SOD1 is used in research to study the enzyme’s structure, function, and role in disease pathogenesis . Additionally, it serves as a potential therapeutic agent to mitigate oxidative damage in clinical settings .
