epitope corresponding to amino acids 25-130 mapping near the N-terminus of SOD-3 of mouse origin
Modification Notes
The superoxide dismutase family is composed of three metalloenzymes (SOD-1, SOD-2 and SOD-3) that catalyze the oxido-reduction of reactive oxygen species (ROS) such as superoxide anion. ROS are implicated in a wide range of degenerative processes, including Alzheimer’s disease, Parkinson’s disease and ischemic heart disease. 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. The SOD-2 precursor is a 222 amino acid protein that is encoded by nuclear chromatin, synthesized in the cytosol and imported posttranslationally into the mitochondrial matrix. SOD-3, also designated extracellular superoxide dismutase (EC-SOD), is an extracellular zinc and copper binding protein that destroys radicals that are toxic to biological systems but that are normally produced within cells. SOD-3 is found in extracellular fluids such as lymph, plasma and synovial fluid.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of SOD-3 of mouse and, to a lesser extent, rat origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 25-130 mapping near the N-terminus of SOD-3 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 25-130 mapping near the N-terminus of SOD-3 of mouse origin