protein

Recombinant Human Superoxide Dismutase

MBS142842

0.02 mg

140 USD

Recombinant Protein

Recombinant Human Superoxide Dismutase

Superoxide Dismutase

SOD Human; Superoxide Dismutase Human Recombinant; Superoxide dismutase [Cu-Zn]; EC 1.15.1.1; SOD1; SOD; ALS; ALS1; IPOA

superoxide dismutase; Superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; superoxide dismutase [Cu-Zn]; Cu/Zn superoxide dismutase; SOD, soluble; epididymis secretory protein Li 44; indophenoloxidase A; superoxide dismutase, cystolic; superoxide dismutase 1, soluble; Superoxide dismutase 1; hSod1

SOD

SOD1; SOD1; ALS; SOD; ALS1; IPOA; hSod1; HEL-S-44; homodimer; hSod1

SODC_HUMAN

E Coli

154

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Lys-Ala-Val.

Greater than 95.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4. Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized SOD although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution SOD should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Solubility: It is recommended to reconstitute the lyophilized SOD in sterile 18M Omega -cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions. Biological Activity: The potency per mg was tested by Pyrogallic Acid method and was found to be more than 10,000 Units/mg.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; Superoxide Dismutase

Description: Recombinant Human Cu/Zn Superoxide Dismutase produced in E Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 154 amino acids and having a total molecular mass of 31,608 Dalton. The Cu/Zn SOD is purified by proprietary chromatographic techniques. Introduction: Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

4507149

NP_000445.1

NM_000454.4

P00441

15,936 Da

AGE/RAGE Pathway (698754); Amyotrophic Lateral Sclerosis (ALS) Pathway (920975); Amyotrophic Lateral Sclerosis (ALS) Pathway (83099); Amyotrophic Lateral Sclerosis (ALS) Pathway (511); Cellular Responses To Stress Pathway (645258); Detoxification Of Reactive Oxygen Species Pathway (1127552); Dopamine Metabolism Pathway (920995); FOXA1 Transcription Factor Network Pathway (137979); Folate Metabolism Pathway (198833); Hemostasis Pathway (106028)

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]

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; response to antibiotic; muscle maintenance; 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; 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; platelet degranulation; sensory perception of sound; ovarian follicle development; regulation of blood pressure; auditory receptor cell stereocilium organization and biogenesis; response to axon injury; 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

0.02 mg

140 USD

0.1 mg

205

1 mg

645