SOD1 recombinant protein

SOD1 Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120953

• Gene Names: SOD1; ALS; SOD; ALS1; IPOA; hSod1; HEL-S-44; homodimer
• Purity: >95% as determined by SDS-PAGE
• Synonyms: SOD1; SOD1 Protein; Human; Recombinant (His Tag); Human SOD1/Superoxide Dismutase Protein (His Tag); ALS Protein; ALS1 Protein; HEL-S-44 Protein; homodimer Protein; hSod1 Protein; IPOA Protein; SOD Protein; superoxide dismutase 1; soluble; SOD1 recombinant protein

• Host: E Coli
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH8.0. 5% trehalose, 5% mannitol and 0.01% Tween80

• Source: Human
• Predicted N Terminal: Met
• Protein Construction: A DNA sequence encoding the human SOD1 (NP_000445.1)(Ala 2-Gln 154) was expressed, with a polyhistide tag at the N-terminus.
• Reconstitution: It is receommended that sterile water (200ul) be added to the vial to prepare a stock solution of 0.25mg/mL. Concentration is mesured by UV-Vis.
• Stability: Samples are stable for up to twelve months from date of receipt at -70°C
• Preparation and Storage: Store it under sterile conditions at -20°C to -80°C upon receiving. Recommended to aliquot the protein into smaller quantities for optimal storage.

SDS-Page

Related Product Information for SOD1 recombinant protein

Background: SOD1 belongs to the Cu-Zn superoxide dismutase family. It 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. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.

References

Murakami K, et al. (2011) SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid beta protein oligomerization and memory loss in mouse model of Alzheimer disease. J Biol Chem. 286(52):44557-68.Thompson M, et al. (2012) Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis. J Neurochem. 120(4):598-610.Magrana© J, et al. (2012) Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J Neurosci. 32(1):229-42.Gertz B, et al. (2012) Nuclear localization of human SOD1 and mutant SOD1-specific disruption of survival motor neuron protein complex in transgenic amyotrophic lateral sclerosis mice. J Neuropathol Exp Neurol. 71(2):162-77.

NCBI and Uniprot Product Information

• NCBI GI #: 4507149
• NCBI GeneID: 6647
• NCBI Accession #: NP_000445.1
• NCBI GenBank Nucleotide #: NM_000454.4
• UniProt Accession #: P00441; Q16669; Q16711; Q16838; Q16839; Q16840; Q6NR85; A6NHJ0; D3DSE4
• Molecular Weight: The recombinant human SOD1 consisting of 161 amino acids and has a calculated molecular mass of 16.8 kDa. It migrates as an approximately 20 kDa band in SDS-PAGE under reducing conditions.
• NCBI Official Full Name: superoxide dismutase
• NCBI Official Synonym Full Names: superoxide dismutase 1, soluble
• NCBI Official Symbol: SOD1
• NCBI Official Synonym Symbols: ALS; SOD; ALS1; IPOA; hSod1; HEL-S-44; homodimer
• NCBI Protein Information: superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; Cu/Zn superoxide dismutase; SOD, soluble; epididymis secretory protein Li 44; indophenoloxidase A; superoxide dismutase, cystolic
• UniProt Protein Name: Superoxide dismutase [Cu-Zn]
• Protein Family: Superoxide dismutase
• UniProt Gene Name: SOD1
• UniProt Synonym Gene Names: hSod1
• UniProt Entry Name: SODC_HUMAN

NCBI Description

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, Jul 2008]

Uniprot Description

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: Oxidoreductase; Mitochondrial; EC 1.15.1.1; Nuclear receptor co-regulator; Apoptosis

Chromosomal Location of Human Ortholog: 21q22.11

Cellular Component: dendrite cytoplasm; extracellular space; protein complex; mitochondrion; extracellular region; mitochondrial intermembrane space; cytosol; nucleoplasm; extracellular matrix; cell soma; mitochondrial matrix; cytoplasm; plasma membrane; peroxisome; cytoplasmic vesicle; 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; activation of MAPK activity; positive regulation of apoptosis; cellular iron ion homeostasis; myeloid cell homeostasis; retrograde axon cargo transport; response to antibiotic; muscle maintenance; 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; positive regulation of cytokine production; response to drug; platelet activation; cell aging; regulation of organ growth; transmission of nerve impulse; 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; sensory perception of sound; platelet degranulation; ovarian follicle development; regulation of blood pressure; response to axon injury; auditory receptor cell stereocilium organization and biogenesis; anterograde axon cargo transport; negative regulation of cholesterol biosynthetic process; 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; regulation of protein kinase activity; blood coagulation; embryo implantation; hydrogen peroxide biosynthetic process

Disease: Amyotrophic Lateral Sclerosis 1