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SOD1 recombinant protein :: Cu/Zn Superoxide Dismutase Homodimer Recombinant Protein

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Catalog # MBS197057
Unit / Price
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  0.02 mg  /  $205 +1 FREE 8GB USB
  0.1 mg  /  $295 +1 FREE 8GB USB
  1 mg  /  $815 +1 FREE 8GB USB
SOD1 recombinant protein
Product Name

Cu/Zn Superoxide Dismutase Homodimer (SOD1), Recombinant Protein

Full Product Name

Recombinant Human Cu/Zn Superoxide Dismutase Homodimer

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 21; NC_000021.8 (33031935..33041244). Location: 21q22.1; 21q22.11
3D Structure
ModBase 3D Structure for P00441
E Coli
Human Cu/Zn Superoxide Dismutase Homodimer
Greater than 95% as determined by SDS- PAGE and RPHPLC.
Lyophilized white powder from a sterile-filtered solution (1mg/ml) in PBS, pH 7.4 Purified by proprietary chromatographic techniques.
Reconstitute lyophilized product in sterile distilled H2O to no less than 100ug/ml which can be further diluted in other aqueous solutions as needed.
Preparation and Storage
Although lyophilized product is stable at room temperature for 3 weeks, it is best stored at or below -20 degree C. After reconstitution, product should be stored at or below -20 degree C. Addition of a carrier protein (such as 0.1% HSA or BSA) is recommended for long-term storage.
Other Notes
Small volumes of SOD1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
SOD1 recombinant protein
Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. It protects a cell from dangerous levels of superoxide. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis (ALS).

Recombinant Human Cu/Zn SOD1 produced in E. coli is a homodimer nonglycosylated polypeptide chain containing 2 x 154 amino acids with a molecular weight of 31.6kDa.
NCBI/Uniprot data below describe general gene information for SOD1. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
15,936 Da[Similar Products]
NCBI Official Full Name
superoxide dismutase
NCBI Official Synonym Full Names
superoxide dismutase 1, soluble
NCBI Official Symbol
NCBI Official Synonym Symbols
ALS; SOD; ALS1; IPOA; hSod1; homodimer
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NCBI Protein Information
superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; SOD, soluble; OTTHUMP00000107278; OTTHUMP00000107279; indophenoloxidase A; Cu/Zn superoxide dismutase; superoxide dismutase, cystolic
UniProt Protein Name
Superoxide dismutase [Cu-Zn]
UniProt Synonym Protein Names
Superoxide dismutase 1
Protein Family
UniProt Gene Name
UniProt Entry Name
NCBI Summary for SOD1
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme 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. Rare transcript variants have been reported for this gene. [provided by RefSeq]
UniProt Comments for SOD1
SOD1: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Homodimer; non-disulfide linked. Homodimerization may take place via the ditryptophan cross-link at Trp-33. The pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5, whereas wild-type protein does not. Belongs to the Cu-Zn superoxide dismutase family.

Protein type: Apoptosis; Oxidoreductase; Nuclear receptor co-regulator; EC; Mitochondrial

Chromosomal Location of Human Ortholog: 21q22.11

Cellular Component: nucleoplasm; dendrite cytoplasm; extracellular matrix; extracellular space; protein complex; mitochondrion; cell soma; mitochondrial matrix; cytoplasm; extracellular region; plasma membrane; mitochondrial intermembrane space; peroxisome; cytoplasmic vesicle; cytosol; nucleus

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; copper ion binding; zinc ion binding; chaperone binding; superoxide dismutase activity; Rac GTPase binding; protein phosphatase 2B binding

Biological Process: positive regulation of catalytic activity; cellular iron ion homeostasis; activation of MAPK activity; positive regulation of apoptosis; myeloid cell homeostasis; retrograde axon cargo transport; muscle maintenance; response to antibiotic; retinal homeostasis; glutathione metabolic process; regulation of mitochondrial membrane potential; neurofilament cytoskeleton organization and biogenesis; positive regulation of superoxide release; negative regulation of neuron apoptosis; placenta development; response to drug; positive regulation of cytokine production; platelet activation; cell aging; transmission of nerve impulse; regulation of organ growth; response to reactive oxygen species; response to ethanol; heart contraction; response to heat; superoxide release; relaxation of vascular smooth muscle; removal of superoxide radicals; locomotory behavior; response to organic substance; platelet degranulation; sensory perception of sound; ovarian follicle development; regulation of blood pressure; response to axon injury; auditory receptor cell stereocilium organization and biogenesis; negative regulation of cholesterol biosynthetic process; anterograde axon cargo transport; response to nutrient levels; response to superoxide; thymus development; regulation of T cell differentiation in the thymus; response to amphetamine; superoxide metabolic process; myelin maintenance in the peripheral nervous system; regulation of multicellular organism growth; response to hydrogen peroxide; response to copper ion; spermatogenesis; blood coagulation; regulation of protein kinase activity; embryo implantation; hydrogen peroxide biosynthetic process

Disease: Amyotrophic Lateral Sclerosis 1
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