Superoxide dismutase-1 (SOD1) is a critical enzyme that plays a vital role in protecting cells from oxidative stress by catalyzing the dismutation of superoxide radicals into oxygen and hydrogen peroxide. This enzyme is highly conserved across species, including humans and mice. The mouse anti-human SOD1 antibody is a monoclonal antibody specifically designed to target and bind to human SOD1, making it a valuable tool in research and diagnostic applications.
SOD1 is a metalloenzyme that typically contains copper and zinc ions at its active site. The enzyme exists as a homodimer, with each subunit consisting of approximately 153 amino acids. The primary function of SOD1 is to catalyze the conversion of superoxide radicals (O2•−) into molecular oxygen (O2) and hydrogen peroxide (H2O2), thereby mitigating the potential damage caused by reactive oxygen species (ROS) in cells.
Mutations in the SOD1 gene are associated with familial amyotrophic lateral sclerosis (fALS), a neurodegenerative disorder characterized by the progressive loss of motor neurons. These mutations can lead to the misfolding and aggregation of SOD1, which exhibits prion-like properties and can propagate the disease . Studies have shown that both wild-type and mutant forms of human SOD1 can induce ALS-like symptoms in transgenic mouse models .
The mouse anti-human SOD1 antibody is a monoclonal antibody that specifically recognizes and binds to human SOD1. This antibody is produced by immunizing mice with human SOD1 protein, followed by the fusion of spleen cells from the immunized mice with myeloma cells to create hybridomas. These hybridomas are then screened for the production of antibodies that specifically target human SOD1.
The mouse anti-human SOD1 antibody is widely used in various research applications, including: