Anti-SOD1 polyclonal antibody

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Recombinant human protein purified from E.coli.

Conjugate

Alternative Names

SOD1; superoxide dismutase 1, soluble; ALS; SOD; ALS1; IPOA; hSod1; homodimer; superoxide dismutase [Cu-Zn]; SOD, soluble; OTTHUMP00000107278; OTTHUMP00000107279; indophenoloxidase A; Cu/Zn superoxide dismutase; superoxide dismutase, cystolic; amyotrophic

Entrez Gene ID

UniProt ID

Antigen Description

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD-1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Pathway

Amyotrophic lateral sclerosis (ALS); FOXA1 transcription factor network; Folate Metabolism; Hemostasis; Huntington"s disease; Oxidative Stress; Peroxisome; Platelet Activation; Platelet degranulation; Prion diseases; Respense to elevated platelet cytosolic Ca2+; Selenium Pathway