Active Recombinant Human Superoxide Dismutase

• Cat.No.: SOD1-8H
• Product Overview: Human SOD is produced in genetically engineered yeast, and purified by ionic exchange chromatography.

Specification

• Description: Cu/Zn Human Superoxide Dismutase is a stable dimer of identical subunits with a combined molecular mass of 32,000 daltons. This enzyme dismutes the superoxide radical to molecular oxygen. This enzyme has been expressed in yeast and purified using sequential chromatography steps. The hSOD is acetylated at its N-terminus.
• Source: yeast
• Species: Human
• Form: 10 mg/ml in water (no additive is added)
• Bio-activity: The specific activity of SOD is 260 U/mg. The enzymatic activity of human SOD is determined by calorimetrically determining the oxidation of a chromophore. This was performed with a commercially available kit called SOD-525 from Bioxytech S.A. (Cedex, France).
• Molecular Mass: 32 KDa (dimeric protein)
• Purity: Over 98% pure by non-reduced SDS gel electrophoresis.
• Stability: Several months at -20°C.
• Storage: Store at -20°C.

Gene Information

• Gene Name: SOD1?superoxide dismutase 1, soluble [?Homo sapiens?(human) ]
• Official Symbol: SOD1
• Synonyms: SOD1; S; SOD; ALS1; IPOA; hSod1; homodimer; superoxide dismutase [Cu-Zn]; SOD, soluble; OTTHUMP00000107278; OTTHUMP00000107279; indophenoloxidase A; Cu/Zn superoxide dismutase; superoxide dismutase, cystolic
• Gene ID: 6647
• mRNA Refseq: NM_000454
• Protein Refseq: NP_000445
• MIM: 147450
• UniProt ID: P00441
• Chromosome Location: 21q22.11
• Pathway: Amyotrophic lateral sclerosis (ALS); FOXA1 transcription factor network; Folate Metabolism; Formation of Platelet plug; Hemostasis; Huntington"s disease; Oxidative Stress
• Function: chaperone binding; copper ion binding; copper ion binding; oxidoreductase activity; protein binding; protein homodimerization activity; protein phosphatase 2B binding; superoxide dismutase activity; zinc ion binding