Browse our Superoxide Dismutase 1, Soluble Proteins (SOD1)

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Superoxide Dismutase 1, Soluble Proteins (SOD1)
On are 107 Superoxide Dismutase 1, Soluble (SOD1) Proteins from 17 different suppliers available. Additionally we are shipping Superoxide Dismutase 1, Soluble Antibodies (513) and Superoxide Dismutase 1, Soluble Kits (75) and many more products for this protein. A total of 710 Superoxide Dismutase 1, Soluble products are currently listed.
Albs, als, als1, B430204E11Rik, CG11793, cSod, Cu, Cu-Zn SOD, CU/ZN-SOD, Cu/ZnSOD, Cu/Zn sod, Cu/Zn superoxide dismutase, CuSOD, cuzn, CuZn-SOD, CuZn-SOD1, CuZnSOD, CuZn SOD, Cu[2+]/Zn[2+]SOD, DKFZP469M1833, Dmel\\CG11793, dSOD1, G, homodimer, hSod1, Ipo-1, Ipo1, ipoa, l(3)68Af', l(3)108, l(3)G, LOC692639, mKIAA4111, Mn SOD, sod, Sod-1, Sod1, sod1-a, SOD1L1, SODC, To, To-1, XSODB, Zn-SOD, ZnSod, Zn Sod, ZSOD
list all proteins Gene Name GeneID UniProt
Mouse SOD1 SOD1 16005 P70389
Rat SOD1 SOD1 79438 P35859
Human SOD1 SOD1 6647 P00441

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Superoxide Dismutase 1, Soluble Proteins (SOD1) by Origin

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Top referenced Superoxide Dismutase 1, Soluble Proteins

  1. Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN2004728 : Kostrzewa, Damian, Müller: Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. in Human genetics 1996 (PubMed)
    Show all 4 references for 2004728

  2. Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN667079 : Banci, Bertini, Boca, Girotto, Martinelli, Valentine, Vieru: SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization. in PLoS ONE 2008 (PubMed)
    Show all 3 references for 667079

More Proteins for Superoxide Dismutase 1, Soluble Interaction Partners

Silk Worm Superoxide Dismutase 1, Soluble (SOD1) interaction partners

Mouse (Murine) Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. the absence of IP3R2 led to increased innate immunity, which may contribute to the decreased survival of the SOD1(G93A) mice.our data indicate that IP3R2 protects against the negative effects of inflammation, suggesting that the increase in IP3R2 expression in ALS patients is a protective response.

  2. the redox regulation of Jmjd3 is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization.

  3. two ALS-linked factors, SQSTM1 (show SQSTM1 Proteins) and ALS2, have distinct but additive protective roles against mutant SOD1-mediated toxicity by modulating neuronal proteostasis possibly through the autophagy-endolysosomal system.

  4. we showed that, in the absence of ERalpha (show ESR1 Proteins), G93A-SOD1 failed to activate OMI (show HTRA2 Proteins) and the proteasome, confirming the ERalpha (show ESR1 Proteins) dependence of the response. Taken together, these results demonstrate the IMS-UPRmt activation in SOD1 familial Amyotrophic lateral sclerosis , and suggest that sex differences in the disease phenotype could be linked to differential activation of the ERa axis of the IMS-UPRmt

  5. The cross-sectional area of the pial arteriolar wall was increased in SOD1 deficiency, and a hyperhomocysteinemic diet sensitized SOD1-deficient mice to this hypertrophic effect. Analysis of of the vascular wall demonstrated a increase in the content of smooth muscle and elastin (show ELN Proteins). We conclude that superoxide is a driver of both cerebral vascular hypertrophy and vasomotor dysfunction in a model of hyperhomocysteinemia.

  6. SOD1 has a role in amyotrophic lateral sclerosis disease phenotype

  7. the damage and satellite cell state of the gastrocnemius muscle in SOD1 knockout mice, was investigated.

  8. Events occurring locally in the skeletal muscle of SOD1 mutant mice contribute to the impairment of CaV1.1 function in ALS muscle independently of innervation status.

  9. G85R-SOD1:YFP inclusion pathology quickly spreads to discrete neurons in the brainstem and midbrain that are synaptically connected to spinal neurons

  10. SOD1 aggregates interact with the cell surface triggering activation of Rac1 and subsequent membrane ruffling permitting aggregate uptake via stimulated macropinocytosis

Caenorhabditis elegans (C. elegans) Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS (show CCS Proteins) for activation

  2. although several long-lived mutants of Caenorhabditis elegans have increased SOD levels, this phenomenon does not correlate with life span or growth rate.

  3. SOD isoforms play no role in lifespan in ad lib or dietary restricted conditions, but mutational inactivation of SOD-1 reduces life extension by cold.

  4. the ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

  5. this suggests that the activity of SOD-1, which so far has been thought to act mainly in cytoplasm, helps to control the detoxification of *O2- also in the mitochondria.

Fruit Fly (Drosophila melanogaster) Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. The functional SOD1 and SOD2 (show SOD2 Proteins) genes knockout and their overexpression in neurons and glial tissue increase the sensitivity of Drosophila melanogaster to oxidative stress conditions.

  2. Expression of zinc-deficient human superoxide dismutase (show SOD2 Proteins) in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.

  3. curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation.

  4. The activity of carbohydrate metabolizing enzymes, lipid and triglyceride concentration, and steady state NADPH:NADP(+) in SOD1-null and control transgenic rescue flies, was analysed.

  5. Overexpression of Cu,ZnSOD and MnSOD (show SOD2 Proteins) in transgenic Drosophila.

  6. Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.

  7. SOD1 and SOD2 (show SOD2 Proteins) provide independent protection to compartment-specific protein iron-sulfur clusters against attack by superoxide generated under oxidative stress

  8. A 1140 base pair region, composed of the single sod1 intron along with exon 2, was found to be essential for permitting spatial and temporal expression patterns that approximate normal endogenous expression.

  9. Cu/Zn superoxide dismutase has a role in preventing spontaneous DNA damage

  10. Instability of superoxide dismutase 1 of Drosophila in mutants deficient for its cognate copper chaperone

Human Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. This study demonstrated that the injection into isolated Aplysia neurons of oligomeric forms of a mutant G85R SOD1 associated with ALS in both humans and transgenic mice reduces net outward K+ current and increases excitability.

  2. sodium channel currents in oocytes expressing either wild-type or mutant (A4V) SOD1 protein

  3. findings indicate that CuZn-SOD is able to response to the hypomagnetic field stress and suggest it a mediator of the hypomagnetic field effect.

  4. Data suggest that Ccs1 activates immature Sod1 by delivering copper and facilitating oxidation of intramolecular disulfide bond in Sod1; Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on the apoenzyme. (Ccs1 = copper chaperone for superoxide dismutase (show CCS Proteins); Sod1 = copper-zinc superoxide dismutase)

  5. The cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis has been described.

  6. propose an alternative pathway of mutant SOD1 misfolding that is responsible for oligomerization in the pathologies of the disease.

  7. In cells that overexpress a genetic variant of SOD1, newly made mutant SOD1 was rapidly captured by pathologic intracellular inclusions.

  8. Findings show that a phosphomimetic mutation, T2D, thermodynamically stabilizes SOD1 even in the context of a strongly SOD1-destabilizing mutation, A4V, one of the most prevalent and aggressive amyotrophic lateral sclerosis -associated mutations. This stabilization protects against formation of toxic SOD oligomers and positively impacts motor neuron survival in cellular assays.

  9. Mutated obese carries of SOD1 -251, SOD2 (show SOD2 Proteins) 47 and CAT -262 are associated with a higher distribution of fat in comparison with obese wild-type carriers.

  10. Steered molecular dynamics analysis was used to study the phenomenon of SOD1 proteopathy in ALS (show IGFALS Proteins), suggests that the increased backbone mobility transforms certain surface regions of the misfolded SOD1 into structural equivalents of the interaction hot spots and has guided the identification of SOD1-derived peptides that bind SOD1 and alter the course of the amyloid aggregation of fALS SOD1 mutants.

Pig (Porcine) Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. CuZnSOD mRNA is a broad-spectrum expression gene, which was detected in brain, heart, spleen, liver, kidney, lung, large intestine, small intestine, spinal cord, muscle, backfat, and stomach

Cow (Bovine) Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability

  2. antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase (show GPX1 Proteins), which show the changes in their expression during improper placental release

  3. Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis.

  4. ALOX5AP (show ALOX5AP Proteins), CPNE3 (show CPNE3 Proteins), IL1R2 (show IL1R2 Proteins), IL6 (show IL6 Proteins), TLR2, TLR4 (show TLR4 Proteins), and THY1 (show THY1 Proteins) were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows.

  5. Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced (show SQSTM1 Proteins) by PGF (show PGF Proteins) during functional luteolysis.

  6. At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase (show CAT Proteins).

  7. Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo (show C9orf3 Proteins)-monomer SOD-1 was calculated.

  8. flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa (show GYPA Proteins). The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.

  9. expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles)

  10. Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions.

Rabbit Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. amyloid and oxidative stress-related disease proteins like SOD 1 is increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.

Zebrafish Superoxide Dismutase 1, Soluble (SOD1) interaction partners

  1. fenofibrate almost completely abolished GM-induced reactive oxygen species generation, which seemed to be mediated at least in part by the restoration of the expression of PPARalphadependent antioxidant enzymes, including catalase (show CAT Proteins) and superoxide dismutase (SOD)-1.

  2. The earliest event in the pathophysiology of amyotrohic lateral sclerosis in the mutant sod1 zebrafish model involves neuronal stress in inhibitory interneurons, resulting from mutant Sod1 expression.

  3. A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a (show ATP7A Proteins), sp1 (show SP1 Proteins) and sod1 in zebrafish.

  4. depresses cathepsin L (show CTSL1 Proteins) activity stimulated by free radicals and prevents otic complications associated with bone erosion

  5. Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). Evidence is presented that SOD protects against paraquat toxicity in fish.

  6. Glia maturation factor-null cells ahow a concurrent decrease in CuZnSOD astrocytes.

Superoxide Dismutase 1, Soluble (SOD1) Protein Profile

Protein Summary

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.

Alternative names and synonyms associated with Superoxide Dismutase 1, Soluble (SOD1)

  • superoxide dismutase 1, soluble (sod1)
  • Superoxide dismutase [Cu-Zn] (SOD1)
  • Cu/Zn superoxide dismutase (A245R)
  • Cu/Zn superoxide dismutase (SOD2.2)
  • Cu/Zn superoxide dismutase (sod1)
  • superoxide dismutase 1, soluble (SOD1)
  • Cu/Zn superoxide dismutase (SOD)
  • insulin-like growth factor binding protein, acid labile subunit (Igfals)
  • Protein SOD-1 (sod-1)
  • Superoxide dismutase (Sod)
  • superoxide dismutase [Cu-Zn]-like (LOC101451855)
  • superoxide dismutase 1, soluble (Sod1)
  • superoxide dismutase 1, soluble (sod1-b)
  • Albs protein
  • als protein
  • als1 protein
  • B430204E11Rik protein
  • CG11793 protein
  • cSod protein
  • Cu protein
  • Cu-Zn SOD protein
  • CU/ZN-SOD protein
  • Cu/ZnSOD protein
  • Cu/Zn sod protein
  • Cu/Zn superoxide dismutase protein
  • CuSOD protein
  • cuzn protein
  • CuZn-SOD protein
  • CuZn-SOD1 protein
  • CuZnSOD protein
  • CuZn SOD protein
  • Cu[2+]/Zn[2+]SOD protein
  • DKFZP469M1833 protein
  • Dmel\\CG11793 protein
  • dSOD1 protein
  • G protein
  • homodimer protein
  • hSod1 protein
  • Ipo-1 protein
  • Ipo1 protein
  • ipoa protein
  • l(3)68Af' protein
  • l(3)108 protein
  • l(3)G protein
  • LOC692639 protein
  • mKIAA4111 protein
  • Mn SOD protein
  • sod protein
  • Sod-1 protein
  • Sod1 protein
  • sod1-a protein
  • SOD1L1 protein
  • SODC protein
  • To protein
  • To-1 protein
  • XSODB protein
  • Zn-SOD protein
  • ZnSod protein
  • Zn Sod protein
  • ZSOD protein

Protein level used designations for SOD1

superoxide dismutase [Cu-Zn] , Cu/Zn superoxide dismutase , superoxide dismutase 1 soluble , superoxide dismutase , Cu/Zn SOD , insulin-like growth factor-binding protein complex acid labile subunit , insulin-like growth factor binding protein complex acid-labile subunit , insulin-like growth factor-binding protein complex acid labile chain , CG11793-PA , CG11793-PD , Cu, Zn superoxide dismutase , Cu-Zn superoxide dismutase , Cu/Zn-Superoxide dismutase , CuZn superoxide dismutase , CuZn-superoxide dismutase , CuZn-superoxide dismutase (SOD)1 , CuZnSOD , Cu[2+] Zn[2+] superoxide dismutase , Cu[2+]Zn[2+] superoxide dismutase , Mn superoxide dismutase , Sod-PA , Sod-PD , complementation group G , copper and zinc SOD , copper-zinc superoxide , copper-zinc superoxide dismutase , cytoplasmic Cu/ZnSOD , dismutase , super oxide dismutase , superoxidase dismutase , superoxide dismutase 1 , superoxide dismutatase , superoxide-dismutase , superoxido dismutase , tetrazolium oxidase , tetrazolium oxidase-1 , SOD, soluble , indophenoloxidase A , superoxide dismutase, cystolic , Cu(2+)-Zn2+ superoxide dismutase , superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult)) , Cu-Zn-superoxide dismutase , Cu,Zn-superoxide dismutase , sod(Cu/Zn) , Cu,Zn superoxide dismutase , superoxide dismutase [Cu-Zn] B

100381040 Xenopus laevis
100499991 Glycine max
918416 Paramecium bursaria Chlorella virus 1
4836692 Scheffersomyces stipitis CBS 6054
100136454 Salmo salar
100172349 Pongo abelii
692639 Bombyx mori
16005 Mus musculus
79438 Rattus norvegicus
174141 Caenorhabditis elegans
39251 Drosophila melanogaster
101451855 Ceratitis capitata
6647 Homo sapiens
20655 Mus musculus
24786 Rattus norvegicus
100033855 Equus caballus
100135622 Cavia porcellus
403559 Canis lupus familiaris
397036 Sus scrofa
281495 Bos taurus
101115136 Ovis aries
100009313 Oryctolagus cuniculus
395938 Gallus gallus
100270717 Ovis aries
449637 Pan troglodytes
100861196 Capra hircus
574096 Macaca mulatta
30553 Danio rerio
394274 Xenopus laevis
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