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.
Formulation
1 mg/ml in 1X PBS; BSA free, sodium azide free
Host
Mouse
Immunogen Region
A portion of amino acids 14-148 from the human protein was used as the immunogen for the SOD1 antibody.
Isotype
Mouse IgG2b, kappa
Species Reactivity
Human
Note
Optimal dilution of the SOD1 antibody should be determined by the researcher.
Uniprot
P00441
Format
Purified
Purity
Protein G affinity chromatography
Storage
Store the SOD1 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
Applications
WB, FACS, IHC-P
Description
Western blot: 2-4ug/ml,Flow cytometry: 1-2ug/million cells,Immunohistochemistry (FFPE): 1-2ug/ml for 30 minutes at RT