Amyotrophic lateral sclerosis 1 (ALS1), Cu/Zn SOD, Cu/Zn Superoxide Dismutase, Epididymis Secretory Protein Li 44, Indophenoloxidase A (IPOA), Superoxide Dismutase [Cu-Zn], Superoxide Dismutase 1 (SOD1)
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 Alzheimers 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.
Immunohistology (Formalin-fixed) (1-2ug/ml for 30 minutes at RT),(Staining of formalin-fixed tissues requires boiling tissue sections in 10mM Citrate Buffer, pH 6.0, for 10-20 min followed by cooling at RT for 20 minutes),
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