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SOD1 (EDI) Antibody

  • WB - SOD1 (EDI) Antibody ASM10466
    Western blot analysis of Mouse Lung showing detection of ~18 kDa SOD1 (EDI) protein using Rabbit Anti-SOD1 (EDI) Polyclonal Antibody (ASM10466). Lane 1: Molecular Weight Ladder. Lane 2: Mouse Lung. Load: 20 µg. Primary Antibody: Rabbit Anti-SOD1 (EDI) Polyclonal Antibody (ASM10466) at 1:1000. Predicted/Observed Size: ~18 kDa.
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P00441
Other Accession CAG46542
Host Rabbit
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Description Rabbit Anti-Human SOD1 (EDI) Polyclonal
Target/Specificity Recognizes a conformation specific epitope where the dimer interface is exposed.
Other Names SEDI Antibody, SOD1 EDI Antibody, Superoxide dismutase 1 Antibody, SOD Antibody, SOD1 exposed dimer interface Antibody
Immunogen N-terminal region of SOD1, exposed dimer interface (EDI)
Purification Protein A Purified
Storage -20ºC
Storage Buffer PBS, 50% glycerol, 0.09% sodium azide
Shipping Temperature Blue Ice or 4ºC
Certificate of Analysis 1 µg/ml of SPC-206 was sufficient for detection of the exposed dimer interface of SOD1 by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
Cellular Localization Cytoplasm
Research Areas
Citations (0)

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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 SOD1 (EDI), which targets an exposed region of the dimer interface (EDI) of SOD1, are useful for determining the conformation of SOD1 in affected tissues (5). This antibody can be used in conjunction with SOD1 (UβB) (SPC-205D) which detects an unfolded beta barrel (UβB) of SOD1.


1. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180.
2. Furukawa Y., and O’Halloran T. (2006) Antioxid Redox Signal. 8(5-6):847-67.
3. Gao B., et al. (2003) Am J Physiol Lung Cell Mol Physiol. 284:L917-L925.
4. Hassan H.M. (1988) Free Radical Biol. Med. 5:377-385.
5. Kerman A., et al. (2010) Acta Neuropathol. 119:335-344.

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Cat# ASM10466
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