SOD1 Monomers

Human Recombinant Superoxide Dismutase 1 (SOD1) Monomers

Product Specifications

Background

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) .

Product Name Alternative

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

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

6647

Swiss Prot

P00441

Accession Number

NP_000445.1

Cellular Locus

Nucleus | Mitochondrion | Cytoplasm

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

Superoxide Dismutase (SOD)

Conjugation

No Tag

Nature

Recombinant

Applications

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

Field of Research

Purification Method

Ion-exchange Purified

Purification

Ion-exchange Purified

Limit Of Detection

Certified >95% pure using SDS-PAGE analysis.

Concentration

Lot/batch specific. See included datasheet.

Purity

>95%

Weight

0.2

Length

Full length

Buffer

PB pH 7.4

Molecular Weight

15.936 kDa

Precautions

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

Additionnal Information

For corresponding PFFs, see catalog# SPR-470

References & Citations

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.

Shipping Conditions

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

Storage Conditions

-80ºC

Notes

For corresponding PFFs, see catalog# SPR-470

Protein Length

Full length

Background Reference 01

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.