Human Superoxide Dismutase Recombinant

Catalog #
90240-A
$130 *
Size: 20 µg
Qty
*US Pricing only. For international pricing, please contact your local distributor.
Purchase
Description

SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residues, and migrates as an approximately 31 kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in E. coli.

Synonyms
SOD1, Superoxide dismutase [Cu-Zn], Superoxide dismutase 1, Amyotrophic Lateral Sclerosis 1, ALS1
Product Info
Storage and Usage
Citations
Species
Human
Host Species/Expression System
E. coli
Purity
≥95% by SDS-PAGE and HPLC
Format
lyophilized protein
Formulation
Lyophilized from a 0.2 µm filtered PBS solution, pH 7.0.
MW
16 kDa
Endotoxin Level
<0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Amino Acids
2–154
Biological Activity
The activity was measured by Pyrogallic Acid method and was found to be not less than 1 x 104 IU/mg.
Genbank #
NM_000454.4
UniProt #
P00441
Background
Cu/Zn Superoxide Dismutase (SOD1) antagonizes IL3 dependent proliferation of cells in culture and reversibly inhibits DNA synthesis of erythroid progenitor cells. SOD1 binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. SOD1 is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis.
References
1. Murakami K, et al. J Amino Acids. 2011,2011:654207.
2. Buettner GR. Anticancer Agents Med Chem. 2011 May 1,11(4):341-6.