| Catalog# |
CE19 |
| Source |
E.coli |
| Description |
Recombinant Human Superoxide Dismutase [Cu-Zn]/SOD1 is produced by our E. coli expression system. The target protein is expressed with sequence (Ala2-Gln154) of Human SOD1 fused with a 6His tag at the N-terminus. |
| Names |
Superoxide Dismutase [Cu-Zn], Superoxide Dismutase 1, hSod1, SOD1 |
| Accession # |
P00441 |
| Formulation |
Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2 |
| Shipping |
The product is shipped on dry ice/ice packs. |
| Storage |
Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles. |
| Purity |
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
| Endotoxin |
Less than 0.1 ng/μg (1 IEU/μg). |
| Amino Acid Sequence |
MGSSHHHHHHSSGLVPRGSHMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHG FHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGD HCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
|
| Background |
Superoxide Dismutase [Cu-Zn] (SOD1) is a soluble cytoplasmic and mitochondrial intermembrane space protein that belongs to the Cu-Zn superoxide dismutase family. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals in the body. SOD1 neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. The enzyme protects the cell against dangerous levels of superoxide. Zinc binding promotes dimerization and stabilizes the native form. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. |
