Browse our anti-Superoxide Dismutase 1, Soluble (SOD1) Antibodies

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anti-Superoxide Dismutase 1, Soluble Antibodies (SOD1)
On are 532 Superoxide Dismutase 1, Soluble (SOD1) Antibodies from 33 different suppliers available. Additionally we are shipping Superoxide Dismutase 1, Soluble Proteins (108) and Superoxide Dismutase 1, Soluble Kits (82) and many more products for this protein. A total of 737 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 antibodies Gene Name GeneID UniProt
Anti-Mouse SOD1 SOD1 16005 P70389
Anti-Rat SOD1 SOD1 79438 P35859
SOD1 6647 P00441

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Top referenced anti-Superoxide Dismutase 1, Soluble Antibodies

  1. Human Polyclonal SOD1 Primary Antibody for ELISA, WB - ABIN190907 : Ghadge, Wang, Sharma, Monti, Bindokas, Stevens, Roos: Truncated wild-type SOD1 and FALS-linked mutant SOD1 cause neural cell death in the chick embryo spinal cord. in Neurobiology of disease 2005 (PubMed)
    Show all 3 references for 190907

  2. Human Polyclonal SOD1 Primary Antibody for IP, IHC - ABIN223175 : Kim, Kim, Hwang, Lee, Shin, Gwag, Koh: Accumulation of labile zinc in neurons and astrocytes in the spinal cords of G93A SOD-1 transgenic mice. in Neurobiology of disease 2009 (PubMed)
    Show all 2 references for 223175

  3. Human Polyclonal SOD1 Primary Antibody for FACS, IF - ABIN652681 : Crapo, Oury, Rabouille, Slot, Chang: Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells. in Proceedings of the National Academy of Sciences of the United States of America 1992 (PubMed)
    Show all 2 references for 652681

  4. Human Polyclonal SOD1 Primary Antibody for IHC, WB - ABIN2782351 : Hays, Naini, He, Mitsumoto, Rowland: Sporadic amyotrophic lateral sclerosis and breast cancer: Hyaline conglomerate inclusions lead to identification of SOD1 mutation. in Journal of the neurological sciences 2006 (PubMed)
    Show all 2 references for 2782351

  5. Arabidopsis thaliana Polyclonal SOD1 Primary Antibody for WB - ABIN3197496 : dAlché: Modelling and mapping of the cardiac electrical field. in Acta cardiologica 1998 (PubMed)

More Antibodies against 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. deletion-rescue experiments show that a respiration-defective mutant of SOD1 is also impaired in its ability to rescue cells from toxicity caused by SOD1 deletion

  2. These findings indicate that a loss of Sig1R function is causative for juvenile amyotrophic lateral sclerosis (ALS16), and collapse of the mitochondria-associated membrane is a common pathomechanism in both Sig1R- and SOD1-linked ALS.

  3. the aberrant mutant SOD1-G3BP1 (show G3BP1 Antibodies) interaction affects stress granule dynamics

  4. 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.

  5. the redox regulation of Jmjd3 (show Kdm6b Antibodies) is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization.

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

  7. we showed that, in the absence of ERalpha (show ESR1 Antibodies), G93A-SOD1 failed to activate OMI (show HTRA2 Antibodies) and the proteasome, confirming the ERalpha (show ESR1 Antibodies) 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

  8. 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 Antibodies). We conclude that superoxide is a driver of both cerebral vascular hypertrophy and vasomotor dysfunction in a model of hyperhomocysteinemia.

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

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

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 Antibodies) 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 (show LRRC15 Antibodies) 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 Antibodies) 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 Antibodies) 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 Antibodies) 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 Antibodies) 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. deletion-rescue experiments show that a respiration-defective mutant of SOD1 is also impaired in its ability to rescue cells from toxicity caused by SOD1 deletion

  2. Factors released in vitro from astrocytes derived from SOD-1 transgenic mice cause spinal motoneuron death and consequent neuromuscular dysfunction in vivo.

  3. This study identified a new pathology hallmark in SOD1G93A ALS mice: a glutamatergic sensory neuron dendropathy restricted to olfactory bulb mitral cells and retinal ganglionic cells.

  4. 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

  5. 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.

  6. 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.

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

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

  9. 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 Antibodies); Sod1 = copper-zinc superoxide dismutase)

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

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

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

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

  4. depresses cathepsin L (show CTSL1 PLURAL_@6154@) 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 Antibodies)-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) antibody
  • Superoxide dismutase [Cu-Zn] (SOD1) antibody
  • Cu/Zn superoxide dismutase (A245R) antibody
  • Cu/Zn superoxide dismutase (SOD2.2) antibody
  • Cu/Zn superoxide dismutase (sod1) antibody
  • superoxide dismutase 1, soluble (SOD1) antibody
  • Cu/Zn superoxide dismutase (SOD) antibody
  • insulin-like growth factor binding protein, acid labile subunit (Igfals) antibody
  • Protein SOD-1 (sod-1) antibody
  • Superoxide dismutase (Sod) antibody
  • superoxide dismutase [Cu-Zn]-like (LOC101451855) antibody
  • superoxide dismutase 1, soluble (Sod1) antibody
  • superoxide dismutase 1, soluble (sod1-b) antibody
  • Albs antibody
  • als antibody
  • als1 antibody
  • B430204E11Rik antibody
  • CG11793 antibody
  • cSod antibody
  • Cu antibody
  • Cu-Zn SOD antibody
  • CU/ZN-SOD antibody
  • Cu/ZnSOD antibody
  • Cu/Zn sod antibody
  • Cu/Zn superoxide dismutase antibody
  • CuSOD antibody
  • cuzn antibody
  • CuZn-SOD antibody
  • CuZn-SOD1 antibody
  • CuZnSOD antibody
  • CuZn SOD antibody
  • Cu[2+]/Zn[2+]SOD antibody
  • DKFZP469M1833 antibody
  • Dmel\\CG11793 antibody
  • dSOD1 antibody
  • G antibody
  • homodimer antibody
  • hSod1 antibody
  • Ipo-1 antibody
  • Ipo1 antibody
  • ipoa antibody
  • l(3)68Af' antibody
  • l(3)108 antibody
  • l(3)G antibody
  • LOC692639 antibody
  • mKIAA4111 antibody
  • Mn SOD antibody
  • sod antibody
  • Sod-1 antibody
  • Sod1 antibody
  • sod1-a antibody
  • SOD1L1 antibody
  • SODC antibody
  • To antibody
  • To-1 antibody
  • XSODB antibody
  • Zn-SOD antibody
  • ZnSod antibody
  • Zn Sod antibody
  • ZSOD antibody

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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