SOD1 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

SOD1 (Superoxide Dismutase 1) is a protein coding gene located on human chromosome 21q22.11. SOD1 is also known as ALS, SOD, ALS1, IPOA, STAHP, hSod1, HEL-S-44 and homodimer. The human SOD1 gene encodes a 15936 Da protein containing 154 amino acids. The SOD1 protein is ubiquitously expressed in liver, kidney and other tissues. Among its related pathways are Neuroscience and Association Between Physico-Chemical Features and Toxicity Associated Pathways. SOD1 is related to protein homodimerization activity and enzyme binding. CCS is an important paralog of SOD1 gene. SOD1 is associated with some diseases, including Amyotrophic Lateral Sclerosis 1 and Spastic Tetraplegia And Axial Hypotonia, Progressive.

SOD1 Protein (1)

    SOD1 Antibody (11)

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      SOD1 cDNA Clone (30)

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      SOD1 Background

      SOD1 belongs to the Cu-Zn superoxide dismutase family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.

      SOD1 References

      • Murakami K, et al. (2011) SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. J Biol Chem. 286(52):44557-68.
      • Thompson M, et al. (2012) Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis. J Neurochem. 120(4):598-610.
      • Magrané J, et al. (2012) Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J Neurosci. 32(1):229-42.
      • Gertz B, et al. (2012) Nuclear localization of human SOD1 and mutant SOD1-specific disruption of survival motor neuron protein complex in transgenic amyotrophic lateral sclerosis mice. J Neuropathol Exp Neurol. 71(2):162-77.

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