Small molecule inhibitors of protein kinases are extensively utilized in sign transduction analysis and are rising as a significant class of medication. Though interpretation of organic outcomes obtained with these reagents critically is determined by their selectivity, environment friendly strategies for proteome-wide evaluation of kinase inhibitor selectivity haven’t but been reported.
Right here, we handle this vital problem and describe a way for figuring out targets of the extensively used p38 kinase inhibitor SB 203580. Immobilization of an acceptable SB 203580 analogue and totally optimized biochemical situations for affinity chromatography permitted the dramatic enrichment and identification of a number of beforehand unknown protein kinase targets of SB 203580.
In vitro kinase assays confirmed that cyclin G-associated kinase (GAK) and CK1 have been nearly as potently inhibited as p38alpha whereas RICK [Rip-like interacting caspase-like apoptosis-regulatory protein (CLARP) kinase/Rip2/CARDIAK] was much more delicate to inhibition by SB 203580. The mobile kinase exercise of RICK, a recognized sign transducer of inflammatory responses, was already inhibited by submicromolar concentrations of SB 203580 in intact cells.
Due to this fact, our outcomes warrant a reevaluation of the huge quantity of knowledge obtained with SB 203580 and may need important implications on the event of p38 inhibitors as antiinflammatory medicine. Primarily based on the procedures described right here, environment friendly affinity purification methods might be developed for different protein kinase inhibitors, offering essential details about their mobile modes of motion.
Weight problems and immune perform relationships.
The immunological processes concerned within the collaborative defence of organisms are affected by dietary standing. Thus, a optimistic continual imbalance between power consumption and expenditure results in conditions of weight problems, which can affect unspecific and particular immune responses mediated by humoral and cell mediated mechanisms.
Moreover, a number of traces of proof have supported a hyperlink between adipose tissue and immunocompetent cells. This interplay is illustrated in weight problems, the place extra adiposity and impaired immune perform have been described in each people and genetically overweight rodents.
Nevertheless, restricted and sometimes controversial info exist evaluating immunity in overweight and non-obese topics in addition to concerning the mobile and molecular mechanisms implicated. Normally phrases, scientific and epidemiological knowledge assist the proof that the incidence and severity of particular forms of infectious diseases are increased in overweight individuals as in comparison with lean people along with the incidence of poor antibody responses to antigens in obese topics.
Leptin would possibly play a key function in linking dietary standing with T-cell perform. The complexities and heterogeneity of the host defences in regards to the immune response in several dietary circumstances affecting the power steadiness require an integral examine of the immunocompetent cells, their subsets and merchandise in addition to particular and unspecific inducer/regulator techniques. On this context, extra analysis is required to make clear the scientific implications of the alterations induced by weight problems on the immune perform.
Runx1 is required for zebrafish blood and vessel growth and expression of a human RUNX1-CBF2T1 transgene advances a mannequin for research of leukemogenesis.
RUNX1/AML1/CBFA2 is important for definitive hematopoiesis, and chromosomal translocations affecting RUNX1 are incessantly concerned in human leukemias. Consequently, the traditional perform of RUNX1 and its involvement in leukemogenesis stay topic to intensive analysis.
To additional elucidate the function of RUNX1 in hematopoiesis, we cloned the zebrafish ortholog (runx1) and analyzed its perform utilizing this mannequin system. Zebrafish runx1 is expressed in hematopoietic and neuronal cells throughout early embryogenesis. runx1 expression within the lateral plate mesoderm co-localizes with the hematopoietic transcription issue scl, and expression of runx1 is markedly diminished within the zebrafish mutants spadetail and cloche.
Transient expression of runx1 in cloche embryos resulted in partial rescue of the hematopoietic defect. Depletion of Runx1 with antisense morpholino oligonucleotides abrogated the event of each blood and vessels, as demonstrated by lack of circulation, incomplete growth of vasculature and the buildup of immature hematopoietic precursors.
The block in definitive hematopoiesis is just like that noticed in Runx1 knockout mice, implying that zebrafish Runx1 has a perform equal to that in mammals. Our knowledge counsel that zebrafish Runx1 capabilities in each blood and vessel growth on the hemangioblast degree, and contributes to each primitive and definitive hematopoiesis. Depletion of Runx1 additionally induced aberrant axonogenesis and irregular distribution of Rohon-Beard cells, offering the primary practical proof of a task for vertebrate Runx1 in neuropoiesis.
To offer a base for analyzing the function of Runx1 in leukemogenesis, we investigated the results of transient expression of a human RUNX1-CBF2T1 transgene [product of the t(8;21) translocation in acute myeloid leukemia] in zebrafish embryos.
Expression of RUNX1-CBF2T1 induced disruption of regular hematopoiesis, aberrant circulation, inside hemorrhages and mobile dysplasia. These defects reproduce these noticed in Runx1-depleted zebrafish embryos and RUNX1-CBF2T1 knock-in mice. The phenotype obtained with transient expression of RUNX1-CBF2T1 validates the zebrafish as a mannequin system to check t(8;21)-mediated leukemogenesis.
From in vivo to in silico biology and again.
The large acquisition of knowledge in molecular and mobile biology has led to the renaissance of an outdated matter: simulations of organic techniques. Simulations, more and more paired with experiments, are being efficiently and routinely utilized by computational biologists to know and predict the quantitative behaviour of complicated techniques, and to drive new experiments.
However, many experimentalists nonetheless think about simulations an esoteric self-discipline just for initiates. Suspicion in the direction of simulations ought to dissipate as the restrictions and benefits of their utility are higher appreciated, opening the door to their everlasting adoption in on a regular basis analysis.
Proteome-wide evaluation of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Submit-translational modification of proteins by lysine acetylation performs vital regulatory roles in residing cells. The budding yeast Saccharomyces cerevisiae is a extensively used unimobile eukaryotic mannequin organism in biomedical analysis.
S. cerevisiae accommodates a number of evolutionary conserved lysine acetyltransferases and deacetylases. Nevertheless, just a few dozen acetylation websites in S. cerevisiae are recognized, presenting a significant impediment for additional understanding the regulatory roles of acetylation on this organism.
Right here we use excessive decision mass spectrometry to determine about 4000 lysine acetylation websites in S. cerevisiae. Acetylated proteins are implicated within the regulation of numerous cytoplasmic and nuclear processes together with chromatin group, mitochondrial metabolism, and protein synthesis.
Bioinformatic evaluation of yeast acetylation websites reveals that acetylated lysines are considerably extra conserved in contrast with nonacetylated lysines. A big fraction of the conserved acetylation websites are current on proteins concerned in mobile metabolism, protein synthesis, and protein folding. Moreover, quantification of the Rpd3-regulated acetylation websites recognized a number of beforehand recognized, in addition to new putative substrates of this deacetylase.
 Superoxide Dismutase Antibody |
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| abx022850-1ml | Abbexa | 1 ml | EUR 1053.6 |
 Human Superoxide Dismutase |
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| 90240-A | BPS Bioscience | 20 µg | EUR 130 |
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Description: SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residues, and migrates as an approximately 31 kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in E. coli. |
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Human Superoxide Dismutase |
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| 90240-B | BPS Bioscience | 100 µg | EUR 205 |
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Description: SOD is a disulfide-linked homodimeric protein consisting of two 154 amino acid residues, and migrates as an approximately 31 kDa protein under non-reducing and as 16 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Superoxide Dismutase mature chain was expressed in E. coli. |
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) Superoxide Dismutase 3 Antibody (SOD3) |
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| F52953-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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Description: SOD3 protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. |
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Superoxide Dismutase 3 Antibody (SOD3) |
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| F49928-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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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. |
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 Superoxide Dismutase 3 Antibody / SOD3 |
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| RQ4091 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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 SOD3 Antibody / Superoxide Dismutase 3 |
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| R30999 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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Superoxide Dismutase 3 Antibody / SOD3 |
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| R31796 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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 Superoxide dismutase 3 Antibody / Sod3 |
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| RQ6518 | NSJ Bioreagents | 100ug | EUR 356.15 |
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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. |
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 Superoxide Dismutase protein |
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| 30R-2714 | Fitzgerald | 100 ug | EUR 542.4 |
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Description: Purified recombinant Human Superoxide Dismutase protein |
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 Superoxide Dismutase 2 antibody |
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| 10R-7478 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 2 antibody |
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Superoxide Dismutase 2 antibody |
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| 10R-7479 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 2 antibody |
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 Superoxide Dismutase 1 antibody |
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| 10R-7482 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 1 antibody |
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Superoxide Dismutase 1 antibody |
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| 10R-7483 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 1 antibody |
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 Superoxide Dismutase 4 antibody |
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| 10R-7484 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 4 antibody |
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Superoxide Dismutase 4 antibody |
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| 10R-7485 | Fitzgerald | 100 ul | EUR 471.6 |
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Description: Mouse monoclonal Superoxide Dismutase 4 antibody |
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 Superoxide Dismutase 1 Antibody |
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| 49350-100ul | SAB | 100ul | EUR 399.6 |
Superoxide Dismutase 1 Antibody |
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| 49350-50ul | SAB | 50ul | EUR 286.8 |
 Superoxide Dismutase 1, Human |
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| LF-P0010 | Abfrontier | 0.5 mg | EUR 242.4 |
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Description: Superoxide Dismutase 1, Human protein |
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 Superoxide Dismutase 2, Human |
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| LF-P0013 | Abfrontier | 0.5 mg | EUR 242.4 |
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Description: Superoxide Dismutase 2, Human protein |
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 Superoxide Dismutase 4, Human |
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| LF-P0020 | Abfrontier | 0.5 mg | EUR 242.4 |
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Description: Superoxide Dismutase 4, Human protein |
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 Superoxide Dismutase 4, mouse |
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| LF-P0410 | Abfrontier | 0.5 mg | EUR 363.6 |
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Description: Superoxide Dismutase 4, mouse protein |
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 Antibody) Superoxide Dismutase (SOD1) Antibody |
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| abx414380-01mg | Abbexa | 0.1 mg | EUR 526.8 |
 Superoxide Dismutase Assay Kit |
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| abx096009-100Assays | Abbexa | 100 Assays | EUR 566.4 |
 SOD, Superoxide Dismutase, human |
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| RC512-12 | Bio Basic | 20ug | EUR 125.26 |
) Chicken Superoxide Dismutase (SOD) |
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| QY-E80142 | Qayee Biotechnology | 96T | EUR 511.2 |
 Antibody (1H12)) Superoxide Dismutase 3 (SOD-3) Antibody (1H12) |
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| 6170-100 | Biovision | each | EUR 483.6 |
 Superoxide Dismutase Standard, 1EA |
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| C098-1EA | Arbor Assays | 1EA | EUR 109 |
 Native Plant Superoxide Dismutase |
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| NATE-1619 | Creative Enzymes | 1g | EUR 324 |
 IgG) Rabbit Anti-human Superoxide Dismutase 3 (SOD3) IgG |
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| SOD32-A | Alpha Diagnostics | 100 ug | EUR 578.4 |
 Antibody) Superoxide Dismutase (SOD-1) Antibody |
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| 3458-100 | Biovision | each | EUR 392.4 |
Superoxide Dismutase (SOD-1) Antibody |
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| 3458-30T | Biovision | each | EUR 175.2 |
) Superoxide Dismutase 2 Antibody (SOD2) |
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| F50529-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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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. |
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) Superoxide Dismutase 1 Antibody (SOD1) |
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| F51318-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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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. |
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 Superoxide Dismutase 2 Antibody / SOD2 |
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| F54062-0.1ML | NSJ Bioreagents | 0.1 ml | EUR 322.15 |
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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] |
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Superoxide Dismutase 2 Antibody / SOD2 |
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| F54485-0.05ML | NSJ Bioreagents | 0.05 ml | EUR 140.25 |
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Description: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
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Superoxide Dismutase 2 Antibody / SOD2 |
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| F54485-0.2ML | NSJ Bioreagents | 0.2 ml | EUR 330.65 |
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Description: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
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Superoxide Dismutase 2 Antibody (SOD2) |
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| F40411-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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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. |
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 SOD1 Antibody Superoxide Dismutase 1 |
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| R30411 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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 SOD2 Antibody Superoxide Dismutase 2 |
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| R30869 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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Superoxide Dismutase 1 Antibody (SOD1) |
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| R31855 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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Superoxide Dismutase 2 Antibody / SOD2 |
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| R31882 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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Superoxide Dismutase 2 Antibody / SOD2 |
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| RQ7037 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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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. |
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Superoxide Dismutase 2 Antibody / SOD2 |
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| RQ5041 | NSJ Bioreagents | 100ul | EUR 356.15 |
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Description: 'Superoxide dismutase [Mn], mitochondrial' destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. [UniProt] |
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 SOD1 Antibody / Superoxide Dismutase 1 |
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| V8968-100UG | NSJ Bioreagents | 100ug | EUR 349.3 |
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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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| V8968-20UG | NSJ Bioreagents | 20ug | EUR 153.3 |
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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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| V8968SAF-100UG | NSJ Bioreagents | 100ug | EUR 349.3 |
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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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| V9162-100UG | NSJ Bioreagents | 100ug | EUR 349.3 |
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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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| 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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| 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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| 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. |
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SOD1 Antibody / Superoxide Dismutase 1 |
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| 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. |
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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. |
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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. |
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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 Bovine Superoxide Dismutase |
|||
| NATE-0675 | Creative Enzymes | 125mg | EUR 324 |
 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 |
 Protein) Superoxide Dismutase [Mn] (SODA) Protein |
|||
| 20-abx261368 | Abbexa |
|
|
 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. |
|||
 Antibody) Superoxide Dismutase 1 (SOD-1) Antibody |
|||
| 6641-100 | Biovision | each | EUR 379.2 |
Superoxide Dismutase 1 (SOD-1) Antibody |
|||
| 6641-30T | Biovision | each | EUR 175.2 |
 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 |
 CLIA Kit) Mouse Superoxide Dismutase 3 (SOD3) CLIA Kit |
|||
| 20-abx190563 | Abbexa |
|
|
 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 [Cu-Zn] Antibody (HRP) |
|||
| 20-abx107845 | Abbexa |
|
|
Superoxide dismutase [Cu-Zn] Antibody (HRP) |
|||
| 20-abx108787 | Abbexa |
|
|
Superoxide dismutase [Cu-Zn] Antibody (HRP) |
|||
| 20-abx108788 | Abbexa |
|
|
 Native Cactus Superoxide Dismutase, 5,000U/g |
|||
| NATE-1868 | Creative Enzymes | 1kg | EUR 440.4 |
 Superoxide Dismutase 1 Conjugated Antibody |
|||
| C49350 | SAB | 100ul | EUR 476.4 |
 Cu/Zn Superoxide Dismutase, Recombinant |
|||
| NATE-1143 | Creative Enzymes | 10mg | EUR 712.8 |
 Antibody) Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
|||
| abx238105-100ug | Abbexa | 100 ug | EUR 661.2 |
Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx218694 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx103950 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx103951 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx103952 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx174663 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx174664 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx174665 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx178501 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx115903 | Abbexa |
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Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| abx448432-100ug | Abbexa | 100 ug | EUR 610.8 |
Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| abx033034-400ul | Abbexa | 400 ul | EUR 627.6 |
Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| abx033034-80l | Abbexa | 80 µl | EUR 343.2 |
Superoxide Dismutase 3, Extracellular (SOD3) Antibody |
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| 20-abx129985 | Abbexa |
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Rpd3 deficiency elevated acetylation of the SAGA (Spt-Ada-Gcn5-Acetyltransferase) complicated subunit Sgf73 on Okay33. This acetylation website is situated inside a crucial regulatory area in Sgf73 that interacts with Ubp8 and is concerned within the activation of the Ubp8-containing histone H2B deubiquitylase complicated. Our knowledge supplies the primary world survey of acetylation in budding yeast, and suggests a wide-ranging regulatory scope of this modification. The offered knowledgeset might function an vital useful resource for the practical evaluation of lysine acetylation in eukaryotes.