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Superoxide Dismutase Recombinant Protein | SOD recombinant protein

Human Superoxide Dismutase Recombinant

Purity
>95%, as determined by SDS-PAGE and HPLC
Synonyms
Superoxide Dismutase; Human Superoxide Dismutase Recombinant; Human Superoxide Dismutase; sod; SOD recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
>95%, as determined by SDS-PAGE and HPLC
Form/Format
SOD was lyophilized from a 0.2 um filtered PBS solution pH 7.0.
Sequence
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ
Sequence Length
154
Domain
SOD
Host Note
Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in Escherichia Coli.
Endotoxin
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/ug (1EU/ug).
Reconstitution
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Molecular Weight Note
Native human Superoxide Dismutase generated by the proteolytic removal of the signal peptide and propeptide,and has a calculated molecular mass of approximately 17 kDa.

SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residue subunits, and migrates as an approximately 31kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE.
Preparation and Storage
The lyophilized protein is stable for at least 2 years from date of receipt at -20 degree C.
Upon reconstitution, this cytokine can be stored in working aliquots at 2 degree - 8 degree C for one month, or at -20 degree C for six months, with a carrier protein without detectable loss of activity.

Avoid repeated freeze/thaw cycles.
Related Product Information for SOD recombinant protein
Superoxide Dismutase has been isolated from media conditioned by a murine marrow-derived cell line (PB6) and from the conditioned medium of cultured mouse marrow cells. It antagonizes IL3 dependent proliferation of cells in culture and reversibly inhibits DNA synthesis of erythroid progenitor cells.
Product Categories/Family for SOD recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
15,936 Da
NCBI Official Full Name
superoxide dismutase
UniProt Protein Name
Superoxide dismutase [Cu-Zn]
Protein Family
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; EC 1.15.1.1; Nuclear receptor co-regulator; Mitochondrial; 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; cellular iron ion homeostasis; positive regulation of apoptosis; myeloid cell homeostasis; retrograde axon cargo transport; muscle maintenance; response to antibiotic; retinal homeostasis; glutathione metabolic process; neurofilament cytoskeleton organization and biogenesis; regulation of mitochondrial membrane potential; 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; response to heat; heart contraction; 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; 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

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Product Notes

The SOD sod1 (Catalog #AAA553106) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ. It is sometimes possible for the material contained within the vial of "Superoxide Dismutase, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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