|Application ||WB, IHC, IF|
|Calculated MW||15936 Da|
|Other Names||Superoxide dismutase [Cu-Zn], Superoxide dismutase 1, hSod1, SOD1|
|Target/Specificity||A synthetic peptide corresponding to residues on human SOD1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SOD1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Destroys radicals which are normally produced within the cells and which are toxic to biological systems.|
|Cellular Location||Cytoplasm. Mitochondrion. Nucleus. Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Cu/Zn superoxide dismutase (SOD1), a major intracellular antioxidant enzyme, metabolizes superoxide radicals to molecular oxygen and hydrogen peroxide (1). SOD1 is primarily a cytosolic protein, and is ubiquitously expressed in many tissues at higher levels than in the brain and spinal cord (1, 2). The structural interplay of the conserved disulfide bond and metal-site occupancy in SOD1 is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry, the subcellular localization, and the susceptibility of the protein to aggregation (3). Defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS) (4).
1. Jun-ichi Niwa, et al. J. Biol. Chem., 282(38):28087-28095, 2007
2. P. Andreas Jonsson, et al. Brain 129: 451-464, 2006
3. Arnesano F, et al. J Biol Chem 279(46):47998-8003, 2004
4. Deng HX, et al. Science 261(5124):1047-51, 1993
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