Antibody Panel to proteins of the superoxide dismutase enzyme family (SOD1, SOD2, SOD3, SOD4)

*   disables radicals

Superoxide dismutase (SOD) is an antioxidant enzyme and as such part of the defense system against reactive oxygen species (ROS). SOD catalyses the dismutation reaction of the superoxide radical anion (O2-) to hydrogen peroxide (H2O2) through glutathione reductase and catalase.

Several classes of SOD have been identified. These include the intracellular copper/zinc SOD (Cu/Zn-SOD, SOD-1), the mitochondrial manganese SOD (Mn-SOD, SOD2) and the extracellular copper/zinc SOD (ECSOD, SOD3).

SOD-1 is found in all eukaryotic species as homodimeric 32 kD enzyme, which does contain one Cu- and one Zn-ion each. SOD1 neutralizes supercharged oxygen molecules (superoxide radicals), which can damage cells if their levels are not controlled. The superoxide dismutase enzyme probably gains new, but harmful, properties when altered by SOD1 mutations. It is unclear why nerve cells in the brain and spinal cord that control muscle movement (motor neurons) are particularly sensitive to SOD1 mutations.

The Mn-containing, tetrameric enzyme SOD2 is localized at the mitochondrial matrix, in close proximity to the primary endogen source for superoxide, the respiratory chain. For this reason it is excellent as mitochondrial marker.

SOD3 is a heparin-binding multimer of dimers, which is expressed primarily in human lung, vessel walls and airways. It is the major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid. Extracellular superoxide dismutase SOD3 (EC-SOD) protects the extracellular space from toxic effect of reactive oxygen intermediates.

SOD4 is a Cu-Chaperon for SOD (CCS), which specifically delivers Cu to SOD1. CCS presumably activates the Cu/Zn SOD by direct insertion of the Cu-cofactor.

Fig. 1: Western blot analysis of tissue lysates with SOD-2 antibody LF-MA0030
Lane 1: HeLa cell lysate
Lane 2: Mouse brain
Lane 3: Ratte brain

Detection and Analysis of SOD

Acris Antibodies offers a vast selection of antibodies, proteins and ELISA kits (see table below), which can be used to analyse the four isoforms of SOD in Western blots and other methods.

Literature

Eisen A, Mezei MM, Stewart HG, Fabros M, Gibson G, Andersen PM. SOD1 gene mutations in ALS patients from British Columbia, Canada: clinical features, neurophysiology and ethical issues in management. Amyotroph Lateral Scler. 2008 Apr; 9(2):108-19.

Proescher JB, Son M, Elliott JL, Culotta VC. Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. Hum Mol Genet. 2008 Jun 15;17(12):1728-37

Available SOD Antibodies

SOD-1 antibody, SOD-2 antibody, SOD-3 antibody, SOD-4 antibody, SOD-1 protein, SOD-2 protein, SOD-3 protein, SOD-4 protein, SOD-1 ELISA Kit, SOD-2 ELISA Kit.

 

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