Rat superoxide dismutase 1, soluble (SOD1) ELISA kit

Code CSB-EL022397RA
Size 96T,5×96T,10×96T How to order?
Trial Size 24T ELISA kits trial application
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Product Details


This Rat SOD1 ELISA Kit was designed for the quantitative measurement of Rat SOD1 protein in serum, plasma, cell culture supernates, tissue homogenates. It is a Sandwich ELISA kit, its detection range is 15.6 pg/mL-1000 pg/mL and the sensitivity is 3.9 pg/mL.

Target Name superoxide dismutase 1, soluble
Alternative Names Sod1 ELISA Kit; Superoxide dismutase [Cu-Zn] ELISA Kit; EC ELISA Kit
Abbreviation SOD1
Uniprot No. P07632
Species Rattus norvegicus (Rat)
Sample Types serum, plasma, cell culture supernates, tissue homogenates
Detection Range 15.6 pg/mL-1000 pg/mL
Sensitivity 3.9 pg/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Metabolism
Assay Principle quantitative
Measurement Sandwich
Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays): CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
To assess the linearity of the assay, samples were spiked with high concentrations of rat SOD1 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
1:200Average %93
Range %88-95
1:400Average %104
Range %100-107
1:800Average %92
Range %87-95
1:1600Average %97
Range %92-100
The recovery of rat SOD1 spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample TypeAverage % RecoveryRange
Serum (n=5) 9389-95
EDTA plasma (n=4)9592-97
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
10002.774 2.767 2.771 2.638
5002.226 2.305 2.266 2.133
2501.737 1.624 1.681 1.548
1251.108 1.088 1.098 0.965
62.50.636 0.628 0.632 0.499
31.20.339 0.321 0.330 0.197
15.60.231 0.224 0.228 0.095
00.130 0.136 0.133  
ELISA Data Analysis Watch ELISA data processing video & download Curve Expert if needed
and FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 3-5 working days


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Target Background

(From Uniprot)
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene References into Functions
  1. Results provide evidence that ALS mutant SOD1 inhibits axonal transport of mitochondria by inducing PINK1/Parkin-dependent Miro1 degradation. PMID: 28973175
  2. SOD1 protein expression is upregulated and associated with greater oxidant production in skeletal muscle from Ts65Dn mice. PMID: 28697486
  3. These results suggest that the superoxide anion may be the cause of the observed oxidative damage to SOD1(G93A) rat neural tissues and that the iron-sulfur clusters may be the source of poorly liganded redox active iron implicated in ALS pathogenesis. Low temperature EPR spectroscopy appears to be a valuable tool in assessing the role of metals in neurodegenerative diseases PMID: 27130034
  4. SOD1 and zinc have roles in methotrexate-induced germ cell toxicity PMID: 28011267
  5. A motility defect in SOD1-G93A was highly correlated with mitochondrial movement. PMID: 27464601
  6. Diabetic testes showed decreased Nrf2, HO-1, SOD1, PCNA, and Bcl-2 expressions whereas increased COX-2, NF-kappaB, MT, IL-6, and p-ERK levels. SOD1 and GPX5 were decreased in the epididymis of diabetic rat, whereas Zn supplementation attenuated these changes. PMID: 27025721
  7. These findings suggest that diabetes increases lipid peroxidation and decreases SOD1 levels, and treadmill exercise can mitigate diabetes-induced oxidative damage in the hippocampus. PMID: 25293488
  8. The found of this study suggest that, from a histological standpoint, the SOD1-G93A rat is a valid model of ALS bulbar symptoms. PMID: 25825172
  9. SOD1 has sequence homology to an antihypertensive snake bradykinin-potentiating peptide. PMID: 26047849
  10. the knockdown of mutant SOD1 in only the motor cortex resulted in a significant delay of disease onset, expansion of lifespan, enhanced survival of spinal motor neurons,and maintenance of neuromuscular junctions PMID: 25411487
  11. These data extend clinical findings of a more rapid disease progression in individuals with bulbar symptoms to the SOD1-G93A rat model of ALS. PMID: 24291387
  12. Data suggest that expression of CuZnSOD/Sod1 (and mitochondrial MnSOD/Sod2) is down-regulated as retinal neurons undergo apoptosis following onset of diabetes/diabetic retinopathy. PMID: 24527463
  13. Results highlight misfolded SOD1 as common to two Amyotrophic lateral sclerosis (ALS) rodent animal models and familial ALS patient lymphoblasts with four different SOD1 mutations. PMID: 23736301
  14. SOD1, constitutively produced and released by microglia, is identified as an essential component of neuroprotection mediated by microglia. PMID: 22572742
  15. both SIRT3 and PGC-1alpha protect against mitochondrial fragmentation and neuronal cell death by mutant SOD1 PMID: 22819776
  16. Xanthine/xanthine oxidase treatment increases SOD1 and SOD2 protein and activity levels in cardiac progenitor cells. PMID: 22758933
  17. CuZn-SOD levels were increased in the hippocampus in OLETF rats. PMID: 22981416
  18. Data indicate that Cu-ZnSod expression decreased upon long reperfusion and trxr1 expression did not vary. PMID: 22377061
  19. Data show that aging is associated with reduction in superoxide dismutase (SOD) Cu/Zn-SOD protein expression and total SOD enzymatic activity in mesenteric lymphatic vessel (MLV). PMID: 22540739
  20. Cu/Zn-SOD activity was not significantly changed in response to vitamin E administration at any time points, whereas Cu/Zn-SOD mRNA levels were significantly increased after longer time points with high doses (30 and 100 mg/kg) of vitamin E. PMID: 22732938
  21. The increased expression of antioxidant SOD1, specifically in hippocampal neurons, will provide protection from age-related cognitive decline. PMID: 21942371
  22. dehydroepiandrosterone treatment did not alter disease progression or survival in SOD1-G93A rats PMID: 22409357
  23. Using gastrocnemius muscles of mice overexpressing human mutant SOD1 (mutSOD1) at different disease stages. PMID: 22178654
  24. expression of Cu,Zn-superoxide dismutase decreased significantly in the dorsal hippocampus (CA1 and CA2) and tended to decrease in ventral regions (CA3 and dentate gyrus) by the 24th hour after 3-fold exposure to hypoxia. PMID: 22451871
  25. The present results suggested that inhibition of Shh signaling pathway exacerbated rat ischemic damage caused by pMCAO, which may be correlated with down-regulated expression of Gli1, Ptch1 and SOD1. PMID: 22133807
  26. Data have shown that different stressors have diverse effect on hepatic CuZnSOD and MnSOD activity as well as on serum CORT level. PMID: 21625958
  27. Thus mitochondrial dysfunction is a key early element in pathogenesis of motor neuron degeneration in transgenic SOD1 rats PMID: 21745570
  28. rat Cu/Zn SOD can be nitrated, a modification that could lead to the depressed activity of this enzyme found in placentas from diabetic rats PMID: 20815790
  29. Results describe changes in SOD1 immunoreactivity associated with lipid peroxidation and inflammatory responses in the hippocampi of STZ-induced type I diabetic rats. PMID: 20924670
  30. most, but not all, properties of SOD1 remain the same with a GFP tag PMID: 20221404
  31. Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability PMID: 20663894
  32. Data indicate that acute and/or chronic stress models have different degrees of influence on serum corticosterone and copper-zinc/manganese superoxide dismutase subcellular protein levels. PMID: 20020182
  33. A significant reduction of Cu,Zn-Sod-1 activity level is observed during fast speed running in the crural diaphragm muscle. PMID: 20134035
  34. results suggest that mutant SOD1 and defective mitochondria create localized dysfunctional domains in motor axons, which may lead to progressive axonopathy in ALS PMID: 19344250
  35. Transcriptional regulation and environmental induction of gene encoding copper- and zinc-containing superoxide dismutase. PMID: 11912919
  36. Levels of Sod1 mRNA were significantly reduced in congestive heart failure following myocardial infarction. PMID: 14575298
  37. Associated with copper deficiency were consistent reductions in immunoreactive SOD in erythrocytes. PMID: 15337829
  38. Medroxyprogesterone acetate inhibits the effect of idarubicin on blood levels of this enzyme. PMID: 15372991
  39. the role of PPARgamma is specific to events occurring during reperfusion, in which to CuZn-SOD is a mediator of neuroprotection PMID: 15618443
  40. respiratory motor neuron loss results in significant electrophysiologic changes and diaphragmatic atrophy in SOD1 G93A rats PMID: 16084734
  41. mutant superoxide dismutase has a role in experimental amyotrophic lateral sclerosis PMID: 16195234
  42. Overexpression of SOD1 in whole lens prevents H2O2-induced oxidative damage (cataract formation) to the lens and subsequent control of gap junctions by protein kinase Cgamma. PMID: 16254550
  43. Levels are not significantly altered in the rat prostate during aging and thus is unlikely to be an important factor in the evolution of epithelial cell hyperplasia. PMID: 16372329
  44. These findings show a heterogeneous expression of Cu/Zn SOD in restricted cell types in the germinative zones and suggest a role for antioxidant Cu/Zn SOD in progenitor cells of the immature rat brain. PMID: 16567040
  45. We hypothesized that LA might induce dissociation of p56(Lck) from CD4, thus leading to its downmodulation. PMID: 16631605
  46. In conclusion, this study demonstrates an age-related decline in Cu/Zn-SOD and IDO activities, the two enzymes responsible for scavenging O2*-. PMID: 16688932
  47. acute and rapid endothelial cell endocytosis of CuZn-SOD, possibly via activation of a receptor-mediated pathway PMID: 17077646
  48. EcSOD, CuZnSOD, catalase, and MMP-2 mRNA expression did not statistically vary between aortic aneurysm and normal tissue PMID: 17196988
  49. Ischemic attack causes a rapid response in hippocampal tissue as well as in the cerebrospinal fluid, represented by an increase in the activity of endogenous antioxidant enzymes SOD and CAT. PMID: 17215005
  50. Data show that activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo. PMID: 17324120

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Subcellular Location Cytoplasm. Nucleus.
Protein Families Cu-Zn superoxide dismutase family
Database Links

KEGG: rno:24786

STRING: 10116.ENSRNOP00000002885

UniGene: Rn.6059

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