SOD1 Protein & Antibody

Superoxide Dismutase 1

SOD1 Products

SOD1 Protein, Recombinant

Molecule	Species	Description	Cat. No
SOD1/Cu/Zn-SOD	Human	SOD1/Cu/Zn-SOD Protein, Recombinant	11727-H07E

SOD1 Antibody

Molecule	Application	Description	Cat. No
Human SOD1/Cu/Zn-SOD	WB, ELISA	SOD1/Cu/Zn-SOD Antibody, Rabbit MAb	11727-R101
Human SOD1/Cu/Zn-SOD	WB, ELISA	SOD1/Cu/Zn-SOD Antibody, Rabbit PAb	11727-RP01
Human SOD1/Cu/Zn-SOD	WB, ELISA	SOD1/Cu/Zn-SOD Antibody, Rabbit PAb (Antigen Affinity Purified)	11727-RP02

SOD1 cDNA Clone

Molecule	Species	Description	Cat. No
SOD1/Cu/Zn-SOD	Human	Homo sapiens SOD1/Cu/Zn-SOD cDNA Clone	HG11727-G

SOD1 Related Areas

Cancer>>Apoptosis>>Oxidative Stress>>SOD1/Cu/Zn-SOD

Enzyme>>Oxidoreductase>>SOD1/Cu/Zn-SOD

SOD1 Alternative Names

SOD1, ALS, ALS1, IPOA, SOD, homodimer [Homo sapiens]

Sod1, B430204E11Rik, Cu/Zn-SOD, CuZnSOD, Ipo-1, Ipo1, MGC107553, SODC, Sod-1 [Mus musculus]

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 Related Studies

1. 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.
2. 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.
3. 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.
4. 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.