Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (2). It works by catalyzing the dismutation of the superoxide radical O2ˉ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (1,4). In general, SODs play a major role in antioxidant defense mechanisms (3). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (2).

Misfolding of SOD1 has been implicated in Amyotrophic lateral sclerosis (ALS). Therefore conformation specific antibodies such as Anti-SOD1 (UβB), which targets an unfolded region of the beta barrel of SOD1, are useful for determining the conformation of SOD1 in affected tissues (5).
This antibody can be used in conjunction with Anti-SOD1 (EDI) (SPC-206D) which detects an exposed dimer interface (EDI) of SOD1.