Browse our Superoxide Dismutase 1, Soluble (SOD1) ELISA Kits

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Superoxide Dismutase 1, Soluble ELISA Kits (SOD1)
On are 75 Superoxide Dismutase 1, Soluble (SOD1) ELISA Kits from 14 different suppliers available. Additionally we are shipping Superoxide Dismutase 1, Soluble Antibodies (523) and Superoxide Dismutase 1, Soluble Proteins (107) and many more products for this protein. A total of 720 Superoxide Dismutase 1, Soluble products are currently listed.
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Top referenced Superoxide Dismutase 1, Soluble ELISA Kits

  1. ABIN2866576 : Pastori, Carnevale, Menichelli, Nocella, Bartimoccia, Novo, Leo, Violi, Pignatelli: Is There an Interplay Between Adherence to Mediterranean Diet, Antioxidant Status, and Vascular Disease in Atrial Fibrillation Patients? in Antioxidants & redox signaling 2016 (PubMed)
    Show all 13 references for 2866576

  2. Human SOD1 ELISA Kit for Sandwich ELISA - ABIN572327 : Neyestani, Ghandchi, Eshraghian, Kalayi, Shariatzadeh, Houshiarrad: Evidence for augmented oxidative stress in the subjects with type 1 diabetes and their siblings: a possible preventive role for antioxidants. in European journal of clinical nutrition 2012 (PubMed)
    Show all 6 references for 572327

  3. Rat (Rattus) SOD1 ELISA Kit for Sandwich ELISA - ABIN416137 : Moor, Tummel, Prather, Jung, Lopez, Connors, Gould: Consequences of age on ischemic wound healing in rats: altered antioxidant activity and delayed wound closure. in Age (Dordrecht, Netherlands) 2014 (PubMed)
    Show all 3 references for 416137

  4. Mouse (Murine) SOD1 ELISA Kit for Sandwich ELISA - ABIN367881 : Lv, Deng, Yu, Wang, Gong, Jia, Wang: Nrf2-ARE signals mediated the anti-oxidative action of electroacupuncture in an MPTP mouse model of Parkinson's disease. in Free radical research 2015 (PubMed)
    Show all 3 references for 367881

More ELISA Kits 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 (show Kdm6b ELISA Kits) is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization.

  3. two ALS-linked factors, SQSTM1 (show SQSTM1 ELISA Kits) and ALS2 (show ALS2 ELISA Kits), 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 ELISA Kits), G93A-SOD1 failed to activate OMI (show HTRA2 ELISA Kits) and the proteasome, confirming the ERalpha (show ESR1 ELISA Kits) 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 ELISA Kits). 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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) 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. demonstrated that enervating the SOD1 electrostatic loop can lead to an experimentally observed gain of interaction (GOI) responsible for the formation of SOD1 amyloid-like filaments

  2. Sod1 upregulation was noted in the R region of the nonaneurysmal type 1 L/R morphotype. Region-specific transcription profiles of Sod on the basis of BAV morphotype deepen our understanding of its associated aortopathy and provide biological insight on the asymmetric dilatation pattern.

  3. 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.

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

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

  6. 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 ELISA Kits); Sod1 = copper-zinc superoxide dismutase)

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

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

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

  10. 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.

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 ELISA Kits), 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 ELISA Kits), CPNE3 (show CPNE3 ELISA Kits), IL1R2 (show IL1R2 ELISA Kits), IL6 (show IL6 ELISA Kits), TLR2 (show TLR2 ELISA Kits), TLR4 (show TLR4 ELISA Kits), and THY1 (show THY1 ELISA Kits) 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 ELISA Kits) by PGF (show PGF ELISA Kits) 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 ELISA Kits).

  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 ELISA Kits)-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 ELISA Kits). The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.

  9. expression profile in follicles: oocytes (SOD1 throughout ooplasm (show NLRP5 ELISA Kits) & 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 ELISA Kits) 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 ELISA Kits), sp1 (show SP1 ELISA Kits) and sod1 in zebrafish.

  4. depresses cathepsin L (show CTSL1 ELISA Kits) 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 (show GMFG ELISA Kits)-null cells ahow a concurrent decrease in CuZnSOD astrocytes.

Superoxide Dismutase 1, Soluble (SOD1) Antigen Profile

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

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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