SOD1 Monomers

Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3) . 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 (2,5) . In general, SODs play a major role in antioxidant defense mechanisms (4) . 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 (3) . The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extra-cellular space (7) . SOD3 can also be distinguished by its heparin-binding capacity (1) . Studies have shown that in vitro, Cu-Zn SOD (SOD1) fibrils are transduced into cells and function as seeds to trigger the aggregation of endogenously expressed SOD1 (9) .

Human Recombinant Superoxide Dismutase 1 (SOD1) Monomers

Superoxide dismutase1 Protein Monomer, ALS1 Protein Monomer, SOD1 Protein Monomer, IPOA Protein Monomer

12352202

Non-hazardous

Non-hazardous

6647

P00441

NP_000445.1

Nucleus | Mitochondrion | Cytoplasm

E. coli

Superoxide Dismutase (SOD)

No Tag

Recombinant

WB | SDS-PAGE | In vivo assay | In vitro assay

Cancer | Oxidative Stress | Cell Signaling | Protein Trafficking | Chaperone Proteins | Neuroscience | Neurodegeneration | ALS Disease

Ion-exchange Purified

Ion-exchange Purified

Certified >95% pure using SDS-PAGE analysis.

Lot/batch specific. See included datasheet.

>95%

0.2

Full length

PB pH 7.4

15.936 kDa

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

For corresponding PFFs, see catalog# SPR-470

1. Adachi T., et al. (1992). Clin. Chim. Acta. 212: 89-102. 2. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180. 3. Furukawa Y., O'Halloran T. (2006). Antioxidants & Redo Signaling. Vol 8, No 5,6. 4. Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol 284: L917-L925. 5. Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385. 6. Kurobe N., et al. (1990) Biomedical Research. 11: 187-194 7. Wispe J.R., et al. (1989) BBA. 994: 30-36. 8. Xiao-Hong Liu., et al. (1993) Brain Research. 625: 29-37. 9. Furukawa Y., et al. (2013) FEBS 587(16): 2500-2505.

Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.

-80ºC

For corresponding PFFs, see catalog# SPR-470

Full length

1. Adachi T., et al. (1992) . Clin. Chim. Acta. 212: 89-102. 2. Barrister J.V., et al. (1987) . Crit. Rev. Biochem. 22:111-180. 3. Furukawa Y., O'Halloran T. (2006) . Antioxidants & Redo Signaling. Vol 8, No 5,6. 4. Gao B., et al. (2003) . Am J Physiol Lung Cell Mol Physiol 284: L917-L925. 5. Hassan H.M. (1988) . Free Radical Biol. Med. 5: 377-385. 6. Kurobe N., et al. (1990) Biomedical Research. 11: 187-194 7. Wispe J.R., et al. (1989) BBA. 994: 30-36. 8. Xiao-Hong Liu., et al. (1993) Brain Research. 625: 29-37. 9. Furukawa Y., et al. (2013) FEBS 587 (16) : 2500-2505.

Nucleus | Mitochondrion | Cytoplasm