Air air pollution publicity YES is a danger OK issue for arrhythmia. The atrioventricular (AV) conduction axis is essential for the passage {of electrical} alerts to ventricles. We investigated whether or not environmental nanoparticles (NPs) attain the AV axis and whether or not they’re related to ultrastructural cell harm. Right here, we show the detection of the form, measurement, and composition of NPs by transmission electron microscopy (TEM) and energy-dispersive X-ray spectrometry (EDX) in 10 topics from Metropolitan Mexico Metropolis (MMC) with a imply age of 25.3 ± 5.9 and a 71-year-old topic with out cardiac pathology.
We discovered that in each case, Fe, Ti, Al, Hg, Cu, Bi, and/or Si spherical or acicular NPs with a imply measurement of 36 ± 17 nm have been current within the AV axis in situ, freely and as conglomerates, throughout the mitochondria, sarcomeres, lysosomes, lipofuscin, and/or intercalated disks and hole junctions of Purkinje and transitional cells, telocytes, macrophages, endothelium, and adjoining atrial and ventricular fibers.
Erythrocytes have been discovered to switch NPs to the endothelium. Purkinje fibers with elevated lysosomal exercise and completely disordered myofilaments and fragmented Z-disks exhibited NP conglomerates in affiliation with hole junctions and intercalated disks. AV conduction axis pathology brought on by environmental NPs is a believable and modifiable danger issue for understanding widespread arrhythmias and reentrant tachycardia. Anthropogenic, industrial, e-waste, and indoor NPs attain pacemaker areas, thereby growing potential mechanisms that disrupt {the electrical} impulse pathways of the center. The cardiotoxic, oxidative, and irregular electrical efficiency results of NPs in pacemaker areas warrant intensive analysis. Cardiac arrhythmias related to nanoparticle results could possibly be preventable.
Intestine microbiome and amyotrophiclateralsclerosis – a scientific assessment of present proof
Amyotrophic lateral sclerosis (ALS), characterised by a lack of motor neurons within the mind and spinal twine, is a comparatively uncommon however at the moment incurable neurodegenerative illness. The worldwide incidence of ALS is estimated as 1.75 per 100,000 person-years and the worldwide prevalence is estimated as 4.1-8.Four per 100,000 people. Contributions from outdoors the central nervous system to the etiology of ALS have been more and more acknowledged.
Intestine microbiome is without doubt one of the most rapidly rising fields of analysis for ALS. On this article, we carried out a complete assessment of the outcomes from present animal and human research, to offer an up-to-date abstract of the present analysis on intestine microbiome and ALS. In short, we discovered comparatively constant outcomes from animal research, suggesting an altered intestine microbiome composition in experimental ALS. Publication bias may nevertheless be a priority. Findings from human research are largely inconclusive.

A number of animal and human research demonstrated the usefulness of intervention with microbial-derived metabolites in modulating the illness development of ALS. We mentioned potential methodological considerations in these research, together with research design, statistical energy, dealing with strategy of biospecimens and sequencing information, in addition to statistical strategies and interpretation of outcomes. Lastly, we made a number of proposals for continued microbiome analysis in ALS, with the goal to offer legitimate, reproducible, and translatable findings. This text is protected by copyright. All rights reserved.
A Easy Excessive Energy, Quick Response Streaming Potential/Present-Primarily based Electrical Nanogenerator Utilizing a Layer of Al 2 O 3 Nanoparticles
Harvesting power from ambient moisture and pure water sources is at the moment of nice curiosity because of the want for standalone self-powered nano/micro-systems. On this work, we report on the event of a cheap nanogenerator based mostly on a carbon paper-Al2O3 nanoparticle layer-carbon paper (CAC) sandwich construction, the place the 3D Al2O3 layer is deposited by way of vacuum filtration. The sort of system can produce an open-circuit voltage (UOC) of as much as Four V and a short-circuit present (ISC) of ∼18 μA with solely an Eight μL water droplet utilized. To our information, that is the best voltage but reported from a single moisture/water-induced electrical energy nanogenerator utilizing strong oxides and carbon-based supplies. A outstanding output energy of 14.Eight μW could be reached with an optimized resistive load.
Superoxide Dismutase 4, Human |
LF-P0020 |
Abfrontier |
0.5 mg |
EUR 242.4 |
Description: Superoxide Dismutase 4, Human protein |
Superoxide Dismutase 4, mouse |
LF-P0410 |
Abfrontier |
0.5 mg |
EUR 363.6 |
Description: Superoxide Dismutase 4, mouse protein |
Superoxide Dismutase 3, mouse |
LF-P0418 |
Abfrontier |
0.5mg |
EUR 363.6 |
Description: Superoxide Dismutase 3, mouse protein |
Superoxide Dismutase Assay Kit |
abx096009-100Assays |
Abbexa |
100 Assays |
EUR 566.4 |
|
SOD, Superoxide Dismutase, human |
RC512-12 |
Bio Basic |
20ug |
EUR 125.26 |
|
Superoxide Dismutase 3 antibody |
10R-7477 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 3 antibody |
Superoxide Dismutase 2 antibody |
10R-7478 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 2 antibody |
Superoxide Dismutase 2 antibody |
10R-7479 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 2 antibody |
Superoxide Dismutase 1 antibody |
10R-7482 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 1 antibody |
Superoxide Dismutase 1 antibody |
10R-7483 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 1 antibody |
Superoxide Dismutase 4 antibody |
10R-7484 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 4 antibody |
Superoxide Dismutase 4 antibody |
10R-7485 |
Fitzgerald |
100 ul |
EUR 471.6 |
Description: Mouse monoclonal Superoxide Dismutase 4 antibody |
Superoxide Dismutase 1 Antibody |
49350-100ul |
SAB |
100ul |
EUR 399.6 |
Superoxide Dismutase 1 Antibody |
49350-50ul |
SAB |
50ul |
EUR 286.8 |
Superoxide Dismutase Standard, 1EA |
C098-1EA |
Arbor Assays |
1EA |
EUR 109 |
Superoxide Dismutase (SOD1) Antibody |
abx414380-01mg |
Abbexa |
0.1 mg |
EUR 526.8 |
|
Dog Superoxide Dismutase ELISA kit |
E08S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Canine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Dog Superoxide Dismutase ELISA kit |
E08S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Canine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Dog Superoxide Dismutase ELISA kit |
E08S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Canine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Rat Superoxide Dismutase ELISA kit |
E02S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Rat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Rat Superoxide Dismutase ELISA kit |
E02S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Rat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Rat Superoxide Dismutase ELISA kit |
E02S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Rat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Pig Superoxide Dismutase ELISA kit |
E07S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Porcine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Pig Superoxide Dismutase ELISA kit |
E07S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Porcine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Pig Superoxide Dismutase ELISA kit |
E07S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Porcine Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Goat Superoxide Dismutase ELISA kit |
E06S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Goat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Goat Superoxide Dismutase ELISA kit |
E06S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Goat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Goat Superoxide Dismutase ELISA kit |
E06S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Goat Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Recombinant E.Coli Superoxide Dismutase |
7-06481 |
CHI Scientific |
5µg |
Ask for price |
Recombinant E.Coli Superoxide Dismutase |
7-06482 |
CHI Scientific |
20µg |
Ask for price |
Recombinant E.Coli Superoxide Dismutase |
7-06483 |
CHI Scientific |
1mg |
Ask for price |
Superoxide Dismutase [Mn] (SODA) Protein |
20-abx261368 |
Abbexa |
-
EUR 4101.60
-
EUR 393.60
-
EUR 276.00
|
|
|
Mouse Superoxide Dismutase ELISA kit |
E03S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Mouse Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Mouse Superoxide Dismutase ELISA kit |
E03S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Mouse Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Mouse Superoxide Dismutase ELISA kit |
E03S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Mouse Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Human Superoxide Dismutase ELISA kit |
E01S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Human Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Human Superoxide Dismutase ELISA kit |
E01S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Human Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Human Superoxide Dismutase ELISA kit |
E01S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Human Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Recombinant Human Superoxide Dismutase |
7-06472 |
CHI Scientific |
20µg |
Ask for price |
Recombinant Human Superoxide Dismutase |
7-06473 |
CHI Scientific |
100µg |
Ask for price |
Recombinant Human Superoxide Dismutase |
7-06474 |
CHI Scientific |
1mg |
Ask for price |
Superoxide Dismutase (SOD-1) Antibody |
3458-100 |
Biovision |
each |
EUR 392.4 |
Superoxide Dismutase (SOD-1) Antibody |
3458-30T |
Biovision |
each |
EUR 175.2 |
Superoxide Dismutase 2 Antibody (SOD2) |
F50529-0.08ML |
NSJ Bioreagents |
0.08 ml |
EUR 140.25 |
Description: SOD2 is a member of the iron/manganese superoxide dismutase family. It is a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. |
Superoxide Dismutase 1 Antibody (SOD1) |
F51318-0.08ML |
NSJ Bioreagents |
0.08 ml |
EUR 140.25 |
Description: SOD1 binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This 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. |
Superoxide Dismutase 3 Antibody (SOD3) |
F52953-0.08ML |
NSJ Bioreagents |
0.08 ml |
EUR 140.25 |
Description: SOD3 protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. |
Superoxide Dismutase 2 Antibody / SOD2 |
F54062-0.1ML |
NSJ Bioreagents |
0.1 ml |
EUR 322.15 |
Description: Superoxide dismutase 2 is a member of the iron/manganese superoxide dismutase family. The SOD2 gene encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. [Wiki] |
Superoxide Dismutase 2 Antibody / SOD2 |
F54485-0.05ML |
NSJ Bioreagents |
0.05 ml |
EUR 140.25 |
Description: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
Superoxide Dismutase 2 Antibody / SOD2 |
F54485-0.2ML |
NSJ Bioreagents |
0.2 ml |
EUR 330.65 |
Description: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
Superoxide Dismutase 2 Antibody (SOD2) |
F40411-0.08ML |
NSJ Bioreagents |
0.08 ml |
EUR 140.25 |
Description: This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. |
Superoxide Dismutase 3 Antibody (SOD3) |
F49928-0.08ML |
NSJ Bioreagents |
0.08 ml |
EUR 140.25 |
Description: SOD3 is a member of the superoxide dismutase(SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. This protein is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
Rabbit Superoxide Dismutase ELISA kit |
E04S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Rabbit Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Rabbit Superoxide Dismutase ELISA kit |
E04S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Rabbit Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Rabbit Superoxide Dismutase ELISA kit |
E04S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Rabbit Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Monkey Superoxide Dismutase ELISA kit |
E09S0012-192T |
BlueGene |
192 tests |
EUR 1524 |
|
Description: A competitive ELISA for quantitative measurement of Monkey Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Monkey Superoxide Dismutase ELISA kit |
E09S0012-48 |
BlueGene |
1 plate of 48 wells |
EUR 624 |
|
Description: A competitive ELISA for quantitative measurement of Monkey Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Monkey Superoxide Dismutase ELISA kit |
E09S0012-96 |
BlueGene |
1 plate of 96 wells |
EUR 822 |
|
Description: A competitive ELISA for quantitative measurement of Monkey Superoxide Dismutase in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. |
Superoxide Dismutase 3 Antibody / SOD3 |
RQ4091 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: SOD3 (Superoxide Dismutase 3), also called Superoxide Dismutase extracellular, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
SOD1 Antibody Superoxide Dismutase 1 |
R30411 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: Superoxide dismutases are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism.Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm. |
SOD2 Antibody Superoxide Dismutase 2 |
R30869 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: Superoxide Dismutase 2, also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that the enzyme is in the distal portion of 6q25. The gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process. |
SOD3 Antibody / Superoxide Dismutase 3 |
R30999 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: Superoxide Dismutase 3 is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al.(1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al.(2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is though to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix(ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
Superoxide Dismutase 3 Antibody / SOD3 |
R31796 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
Superoxide Dismutase 1 Antibody (SOD1) |
R31855 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: Superoxide dismutases (SOD) are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism.Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm. |
Superoxide Dismutase 2 Antibody / SOD2 |
R31882 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: SOD2 (Superoxide Dismutase 2), also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that SOD2 is in the distal portion of 6q25. The SOD2 gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human SOD2 gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process. |
Superoxide dismutase 3 Antibody / Sod3 |
RQ6518 |
NSJ Bioreagents |
100ug |
EUR 356.15 |
Description: SOD3 (SUPEROXIDE DISMUTASE 3), also called SUPEROXIDE DISMUTASE, EXTRACELLULAR, EC-SOD, and Cu-Zn, is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Hendrickson et al. (1990) mapped the SOD3 gene to 4pter-q21 by a study of somatic cell hybrids. Stern et al. (2003) narrowed the assignment to 4p15.3-p15.1 by somatic cell and radiation hybrid analysis, linkage mapping, and FISH. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM. |
Superoxide Dismutase 2 Antibody / SOD2 |
RQ7037 |
NSJ Bioreagents |
100 ug |
EUR 356.15 |
Description: SOD2 (Superoxide Dismutase 2), also called IPO-B or MNSOD, is a mitochondrial matrix enzyme that scavenges oxygen radicals produced by the extensive oxidation-reduction and electron transport reactions occurring in mitochondria. This gene is a member of the iron/manganese superoxide dismutase family. Using a somatic cell hybrid panel containing different segments of chromosome 6, they demonstrated that SOD2 is located in the region 6q25.3-qter which, together with the FISH analysis, indicated that SOD2 is in the distal portion of 6q25. The SOD2 gene encodes an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation. Adeno-associated viral delivery of the human SOD2 gene resulted in suppression of optic nerve degeneration and rescue of retinal ganglion cells. The findings suggested that reactive oxygen species contributed to retinal cell death and optic nerve damage in mice with complex I deficiency, and that expression of SOD2 attenuated the disease process. |
Superoxide Dismutase 2 Antibody / SOD2 |
RQ5041 |
NSJ Bioreagents |
100ul |
EUR 356.15 |
Description: 'Superoxide dismutase [Mn], mitochondrial' destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. [UniProt] |
SOD1 Antibody / Superoxide Dismutase 1 |
V8968-100UG |
NSJ Bioreagents |
100ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8968-20UG |
NSJ Bioreagents |
20ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8968SAF-100UG |
NSJ Bioreagents |
100ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V9162-100UG |
NSJ Bioreagents |
100ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V9162-20UG |
NSJ Bioreagents |
20ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V9162SAF-100UG |
NSJ Bioreagents |
100ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V3869-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V3869-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V3869SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8619-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8619-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8619SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8620-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8620-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8620SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8621-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8621-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8621SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8622-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8622-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8622SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8623-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8623-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8623SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8624-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8624-20UG |
NSJ Bioreagents |
20 ug |
EUR 153.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
SOD1 Antibody / Superoxide Dismutase 1 |
V8624SAF-100UG |
NSJ Bioreagents |
100 ug |
EUR 349.3 |
Description: Cu-Zn superoxide dismutase-1 (SOD-1) is a well-characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Enzymatically, SOD-1 facilitates the dismutation of oxygen radicals to hydrogen peroxide and also catalyzes pro-oxidant reactions, which include the peroxidase activity and hydroxyl radical generating activity. SOD-1 is ubiquitously expressed in somatic cells and functions as a homodimer. Defects in the gene encoding SOD-1 have been implicated in the progression of neurological diseases, including amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the loss of spinal motor neurons, Down syndrome and Alzheimer s disease. In familial ALS, several mutations in SOD-1 predominate, resulting in the loss of zinc binding, the loss of scavenging activity of SOD-1, and correlate with an increase in neurotoxicity and motor neuron death. |
Native Cactus Superoxide Dismutase, 5,000U/g |
NATE-1868 |
Creative Enzymes |
1kg |
EUR 440.4 |
Cu/Zn Superoxide Dismutase, Recombinant |
NATE-1143 |
Creative Enzymes |
10mg |
EUR 712.8 |
Recombinant Human Superoxide Dismutase-1 |
7-06475 |
CHI Scientific |
5µg |
Ask for price |
Recombinant Human Superoxide Dismutase-1 |
7-06476 |
CHI Scientific |
25µg |
Ask for price |
Recombinant Human Superoxide Dismutase-1 |
7-06477 |
CHI Scientific |
1mg |
Ask for price |
Recombinant Human Superoxide Dismutase-2 |
7-06478 |
CHI Scientific |
5µg |
Ask for price |
Recombinant Human Superoxide Dismutase-2 |
7-06479 |
CHI Scientific |
25µg |
Ask for price |
Recombinant Human Superoxide Dismutase-2 |
7-06480 |
CHI Scientific |
1mg |
Ask for price |
Rat Superoxide Dismutase (SOD) ELISA Kit |
20-abx258686 |
Abbexa |
-
EUR 9493.20
-
EUR 5058.00
-
EUR 1167.60
|
- 10 × 96 tests
- 5 × 96 tests
- 96 tests
|
|
Dog Superoxide Dismutase (SOD) ELISA Kit |
20-abx585379 |
Abbexa |
-
EUR 9567.60
-
EUR 5095.20
-
EUR 1177.20
|
- 10 × 96 tests
- 5 × 96 tests
- 96 tests
|
|
Mouse Superoxide dismutase [Cu-Zn] (Sod1) |
1-CSB-YP022397MO |
Cusabio |
-
EUR 604.80
-
EUR 318.00
-
EUR 2198.40
-
EUR 915.60
-
EUR 1459.20
-
EUR 400.80
|
- 100ug
- 10ug
- 1MG
- 200ug
- 500ug
- 50ug
|
|
Description: Recombinant Mouse Superoxide dismutase [Cu-Zn](Sod1) expressed in Yeast |
Mouse Superoxide dismutase [Cu-Zn] (Sod1) |
1-CSB-EP022397MO |
Cusabio |
-
EUR 606.00
-
EUR 318.00
-
EUR 2192.40
-
EUR 919.20
-
EUR 1461.60
-
EUR 402.00
|
- 100ug
- 10ug
- 1MG
- 200ug
- 500ug
- 50ug
|
|
Description: Recombinant Mouse Superoxide dismutase [Cu-Zn](Sod1) expressed in E.coli |
Fish Superoxide Dismutase(SOD)ELISA kit |
CSB-E15929Fh-24T |
Cusabio |
1 plate of 24 wells |
EUR 198 |
|
Description: Quantitativecompetitive ELISA kit for measuring Fish Superoxide Dismutase (SOD) in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price. |
Fish Superoxide Dismutase(SOD)ELISA kit |
1-CSB-E15929Fh |
Cusabio |
-
EUR 1080.00
-
EUR 6571.20
-
EUR 3480.00
|
- 1 plate of 96 wells
- 10 plates of 96 wells each
- 5 plates of 96 wells each
|
|
Description: Quantitativecompetitive ELISA kit for measuring Fish Superoxide Dismutase(SOD) in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits. |
An LED with a working voltage of 3-3.2 V can function for a short while with the facility from a single CAC system uncovered to at least one Eight μL water droplet. Moreover, a CAC generator adsorbing as little as 2 μL water droplets each Three min may give a UOC of three.63 V. We present that CAC units present a sturdy electrical output over greater than 200 wet-dry cycles with none deterioration in efficiency.
These items show a lot promise as cost-effective electrical energy mills for harvesting power from pure sources like rainwater, faucet water, snow runoff, and dew. The response time of CAC units could be as quick as 10-100 ms, making them very best for purposes as self-powered water detectors. The era of energy on this system arises from the streaming present. To help within the optimization of those units, we’ve analyzed how their response is said to such components as layer thickness, time interval between software of water droplets, and the amount of every water droplet.