Browse our Superoxide Dismutase 1, Soluble Proteins (SOD1)

Full name:: Superoxide Dismutase 1, Soluble Proteins (SOD1)

On www.antibodies-online.com are 103 Superoxide Dismutase 1, Soluble (SOD1) Proteins from 19 different suppliers available. Additionally we are shipping Superoxide Dismutase 1, Soluble Antibodies (619) and Superoxide Dismutase 1, Soluble Kits (103) and many more products for this protein. A total of 842 Superoxide Dismutase 1, Soluble products are currently listed.

Synonyms:: als, als1, B430204E11Rik, CG11793, cSod, Cu, Cu-Zn SOD, Cu/Zn-SOD, Cu/Zn sod, Cu/ZnSOD, Cu/Zn superoxide dismutase, CuSOD, cuzn, CuZn-SOD, CuZn-SOD1, CuZn SOD, CuZnSOD, 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, Mn SOD, sod, Sod-1, sod1, sod1-a, SOD1L1, SODC, To, To-1, XSODB, Zn-SOD, Zn Sod, ZnSod, ZSOD

list all proteins	Gene Name	GeneID	UniProt
Human SOD1	SOD1	6647	P00441
Mouse SOD1	SOD1	20655	P08228
Rat SOD1	SOD1	24786	P07632
Show all synonyms

Superoxide Dismutase 1, Soluble Proteins (SOD1) by Origin

Select your origin of interest

Relevant Pathways for Superoxide Dismutase 1, Soluble Proteins

More product categories related to Superoxide Dismutase 1, Soluble Protein

Top referenced Superoxide Dismutase 1, Soluble Proteins

Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN5777061 : Luchinat, Barbieri, Rubino, Kozyreva, Cantini, Banci: In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. in Nature communications 2014 (PubMed)

More Proteins for Superoxide Dismutase 1, Soluble Interaction Partners

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

Human Superoxide Dismutase 1, Soluble (SOD1) interaction partners

The mutant human SOD1-G93A protein induced axonal and myelin degeneration during the progression of Amyotrophic Lateral Sclerosis in a mouse model and participated in axon remyelination and regeneration in response to injury.
SOD1 oligomer and not the mature form of aggregated fibril is critical for the neurotoxic effects in the model of amyotrophic lateral sclerosis.
Data suggest that serum SOD1 levels are decreased in patients with controlled or uncontrolled acromegaly as compared to healthy subjects; in acromegaly, SOD1 levels are not associated with MnSOD/SOD2 (show SOD2 Proteins) polymorphisms.
Ovariectomy resulted in earlier disease onset and attenuated the anti-inflammatory and anti-apoptotic actions of estrogen in hSOD1-G93A transgenic mice.
a measure of hydrogen bond stability in conformational states was studied with elastic network analysis of 35 SOD1 mutants.
The genetic mutations of SOD1 caused amyotrophic lateral sclerosis
the study provides a better understanding over the profound effect of mutation on SOD1, both structurally and functionally, using computational approaches.
SOD1 amino acid residues forming these pathogenic hydrogen bonds are found in zinc-binding and electrostatic loops as well as at zinc-binding sites and are in contact with SOD1 aggregates, which implies that these regions are sensitive to perturbations from pathogenic mutations.
show a clear variation of the different SOD1 mutants to associate with mitochondrial-enriched fractions with a correlation between mutation severity and this association
Study shows that in senile cataracts, SOD1 expression decreased significantly. Both H3 and H4 were deacetylated at -600 bp of the SOD1 promoter of cataract lenses, and hypoacetylated at -1500, -1200, and -900 bp. In hypoacetylated histones, the hypoacetylation pattern differed among the cataracts sub-types. Further functional data provide evidence that histone acetylation plays an essential role in the regulation of SOD1.

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

the cytosolic SOD-null syndrome is largely consistent across sex and genetic background, but also significantly influenced by both.
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.
Expression of zinc-deficient human superoxide dismutase (show SOD2 Proteins) in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.
curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation.
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.
Overexpression of Cu,ZnSOD and MnSOD (show SOD2 Proteins) in transgenic Drosophila.
Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.
SOD1 and SOD2 (show SOD2 Proteins) provide independent protection to compartment-specific protein iron-sulfur clusters against attack by superoxide generated under oxidative stress
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.
Cu/Zn superoxide dismutase has a role in preventing spontaneous DNA damage

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

Results support the concept that impaired redox signaling, rather than oxidative damage, in peripheral nerve plays a key role in muscle loss in Sod1(-/-) mice and potentially sarcopenia during aging
This evidence favours mutant SOD1-containing astrocytes releasing destructive species that alter the biology of adjacent astrocytes
Given the close association of stress granules and TDP-43 (show TARDBP Proteins), we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 (show TARDBP Proteins) cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 (show TARDBP Proteins) to the cytoplasm where it was still accumulated after 48 h.
Distinct roles for motor neuron autophagy early and late in the SOD1(G93A) mouse model of ALS.
It was observed that global AQP4 (show AQP4 Proteins) expression increased in the spinal cord of SOD1G93A mice as the disease progressed. However, AQP4 (show AQP4 Proteins) polarization decreased as the disease progressed, and AQP4 (show AQP4 Proteins) polarized localization at the endfeet of astrocytes was decreased in the spinal ventral horn of SOD1G93A mice at the disease onset and end stages.
Superoxide dismutase 1 mutation is associated with amyotrophic lateral sclerosis.
Restrictive Lung Disease in the Cu/Zn Superoxide-Dismutase 1 G93A Amyotrophic Lateral Sclerosis Mouse Model.
Endogenous MIF (show MIF Proteins) reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of amyotrophic lateral sclerosis.
This study indicates that axonal and neuromuscular junction degeneration in the SOD1 model of amyotrophic lateral sclerosis is a complex and evolving sequence of events
In this newborn mouse lung hypoxia-reoxygenation model, we found downregulation of genes of mediators of inflammation, an antiapoptotic gene expression pattern, and downregulation of DNA glycosylases. Sod1 and Il1b (show IL1B Proteins) were significantly differentially expressed when comparing reoxygenation using 60% O2 with air.

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

The results showed that 60-min ischemia of the porcine uterus conducted at the mid-secretory estrous phase caused decreased HIF-1alpha (show HIF1A Proteins) and increased SOD-2 (show SOD2 Proteins) gene expression.
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

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

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.

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

These data suggest that SOD1 mutants are removed from the nucleus by CRM1 (show XPO1 Proteins) as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.
the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS (show CCS Proteins) for activation
although several long-lived mutants of Caenorhabditis elegans have increased SOD levels, this phenomenon does not correlate with life span or growth rate.
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.
the ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
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.

Zebrafish Superoxide Dismutase 1, Soluble (SOD1) interaction partners

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.
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.
A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a (show ATP7A Proteins), sp1 (show SP1 Proteins) and sod1 in zebrafish.
depresses cathepsin L activity stimulated by free radicals and prevents otic complications associated with bone erosion
Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). Evidence is presented that SOD protects against paraquat toxicity in fish.
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)

Cu/Zn superoxide dismutase (SOD)
superoxide dismutase 1 (SOD1)
Superoxide dismutase 1 (Sod1)
superoxide dismutase 1, soluble (SOD1)
superoxide dismutase 1, soluble (sod1)
superoxide dismutase 1 S homeolog (sod1.S)
superoxide dismutase 1, soluble (Sod1)
superoxide dismutase 1 (Sod1)
Superoxide dismutase [Cu-Zn] (sod-1)
Superoxide dismutase [Cu-Zn] (SOD1)
superoxide dismutase 1 L homeolog (sod1.L)
superoxide dismutase [Cu-Zn] (LOC101115136)
superoxide dismutase Sod1 (sod1)

als protein
als1 protein
B430204E11Rik protein
CG11793 protein
cSod protein
Cu protein
Cu-Zn SOD protein
Cu/Zn-SOD protein
Cu/Zn sod protein
Cu/ZnSOD protein
Cu/Zn superoxide dismutase protein
CuSOD protein
cuzn protein
CuZn-SOD protein
CuZn-SOD1 protein
CuZn SOD protein
CuZnSOD 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
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
Zn Sod protein
ZnSod protein
ZSOD protein

Protein level used designations for SOD1

, , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , Cu/Zn SOD Cu/Zn superoxide dismutase SOD, soluble indophenoloxidase A superoxide dismutase [Cu-Zn] superoxide dismutase, cystolic 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 superoxide dismutase 1 superoxide dismutatase superoxide-dismutase superoxido dismutase tetrazolium oxidase tetrazolium oxidase-1 superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult)) superoxide dismutase 1 soluble Cu(2+)-Zn2+ superoxide dismutase Cu-Zn-superoxide dismutase Cu,Zn-superoxide dismutase Cu,Zn superoxide dismutase superoxide dismutase [Cu-Zn] B sod(Cu/Zn)

GENE ID	SPECIES
692639	Bombyx mori
6647	Homo sapiens
39251	Drosophila melanogaster
395938	Gallus gallus
100033855	Equus caballus
100136454	Salmo salar
100172349	Pongo abelii
100270717	Ovis aries
100381040	Xenopus laevis
20655	Mus musculus
24786	Rattus norvegicus
403559	Canis lupus familiaris
397036	Sus scrofa
281495	Bos taurus
100009313	Oryctolagus cuniculus
100135622	Cavia porcellus
174141	Caenorhabditis elegans
100499991	Glycine max
574096	Macaca mulatta
449637	Pan troglodytes
394274	Xenopus laevis
101115136	Ovis aries
100861196	Capra hircus
30553	Danio rerio
2542128	Schizosaccharomyces pombe 972h-

Selected quality suppliers for Superoxide Dismutase 1, Soluble Proteins (SOD1)

Did you look for something else?

Phone:	+1 877 302 8632
Fax:	+1 888 205 9894 (Toll-free)
E-Mail:	orders@antibodies-online.com

Show all Superoxide Dismutase 1, Soluble Proteins (SOD1) with Pubmed References