Formalin-fixed, paraffin-embedded human Placenta stained with Superoxide Dismutase 1 Mouse Monoclonal Antibody (SOD1/2089).
SDS-PAGE Analysis Purified Superoxide Dismutase 1 Mouse Monoclonal Antibody (SOD1/2089). Confirmation of Integrity and Purity of Antibody.
Analysis of Protein Array containing more than 19,000 full-length human proteins using Superoxide Dismutase 1 Mouse Monoclonal Antibody (SOD1/2089).
Known Applications & Suggested Dilutions
Host / Ig Isotype
Mol. Weight of Antigen
Specificity & Comments
Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death.