Mouse Super Oxidase Dimutase,SOD ELISA Kit

Code CSB-E08556m
Size 96T
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Trial Size 24T ELISA Kit Trial Size (Only USD$150/ kit)
* The sample kit cost can be deducted from your subsequent orders of 96T full size kits of the same analyte at 1/5 per kit, until depleted in 6 months. Apply now

Product Details

Target Name
superoxide dismutase 1, soluble
Alternative Names
Sod1 ELISA Kit; Superoxide dismutase [Cu-Zn] ELISA Kit; EC ELISA Kit
Uniprot No.
Mus musculus (Mouse)
Sample Types
serum, plasma, tissue homogenates
Detection Range
5.4 pg/mL-4000 pg/mL
5.4 pg/mL
Assay Time
Sample Volume
Detection Wavelength
450 nm
Research Area
Typical Data
Materials provided
  • A micro ELISA plate ---The 96-well plate has been pre-coated with an anti-mouse SOD antibody. This dismountable microplate can be divided into 12 x 8 strip plates.
  • Two vials lyophilized standard ---Dilute a bottle of the standard at dilution series, read the OD values, and then draw a standard curve.
  • One vial Biotin-labeled SOD antibody (100 x concentrate) (120 μl/bottle) ---Act as the detection antibody.
  • One vial HRP-avidin (100 x concentrate) (120 μl/bottle) ---Bind to the detection antibody and react with the TMB substrate to make the solution chromogenic.
  • One vial Biotin-antibody Diluent (15 ml/bottle) ---Dilute the Biotin-antibody.
  • One vial HRP-avidin Diluent (15 ml/bottle) ---Dilute the HRP-avidin solution.
  • One vial Sample Diluent (50 ml/bottle)---Dilute the sample to an appropriate concentration.
  • One vial Wash Buffer (25 x concentrate) (20 ml/bottle) ---Wash away unbound or free substances.
  • One vial TMB Substrate (10 ml/bottle) ---Act as the chromogenic agent. TMB interacts with HRP, eliciting the solution turns blue.
  • One vial Stop Solution (10 ml/bottle) ---Stop the color reaction. The solution color immediately turns from blue to yellow.
  • Four Adhesive Strips (For 96 wells) --- Cover the microplate when incubation.
  • An instruction manual
Materials not provided
  • A microplate reader capable of measuring absorbance at 450 nm, with the correction wavelength set at 540 nm or 570 nm.
  • An incubator can provide stable incubation conditions up to 37°C±5°C.
  • Centrifuge
  • Vortex
  • Squirt bottle, manifold dispenser, or automated microplate washer
  • Absorbent paper for blotting the microtiter plate
  • 50-300ul multi-channel micropipette
  • Pipette tips
  • Single-channel micropipette with different ranges
  • 100ml and 500ml graduated cylinders
  • Deionized or distilled water
  • Timer
  • Test tubes for dilution
and FAQs
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx

The Mouse Super Oxidase Dimutase (SOD) ELISA Kit allows for the detection and quantification of SOD in mouse serum, plasma, or tissue homogenates. This kit has high sensitivity, excellent specificity, precision less than 10%, and consistency between batches. It employs the sandwich ELISA mechanism and enzyme-substrate chromogenic reaction to achieve the detection. The solution color develops in proportion to the amount of SOD in the sample, and the color intensity can be measured at 450 nm via a microplate reader.

SOD is a homo-dimeric metalloprotein that catalyzes the dismutation of the free superoxide (O2−) radical into molecular oxygen (O2) and hydrogen peroxide (H2O2). It primarily localizes to the cytoplasm but is also found in the nucleus and the intermembrane space (IMS) of the mitochondria. SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. The dismutase activity of SOD may be essential to the accumulation of reactive oxygen species (ROS) and misfolded proteins in the IMS of the mitochondria. Additionally, heterozygous variants in SOD are a common cause of familial amyotrophic lateral sclerosis (ALS), a form of motor neuron disease.


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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. These findings suggest unexpected specificity, mediated by both the primary protein pathology and cellular context, in the induced "secondary aggregation" of a mutant form of SOD1 that could be viewed as a reporter of proteostatic function PMID: 29776378
  2. Presence of mutated SOD1 protein affects the MHC class I molecules expression and is associated with facial injured motoneurons. PMID: 29943955
  3. DKO mice spontaneously develop severe liver failure at a relatively young stage, they have the potential for use as a model for hepatic disorders and for testing other potential treatments. PMID: 30050648
  4. These results suggest that overexpression of SQSTM1 in SOD1 (H46R) mice accelerates disease onset by compromising the protein degradation pathways. PMID: 29843805
  5. Results support the concept that impaired redox signaling, rather than oxidative damage, in peripheral nerve plays a key role in muscle loss in Sod1(-/-) mice and potentially sarcopenia during aging PMID: 29065712
  6. This evidence favours mutant SOD1-containing astrocytes releasing destructive species that alter the biology of adjacent astrocytes PMID: 28861673
  7. Given the close association of stress granules and TDP-43, we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 to the cytoplasm where it was still accumulated after 48 h. PMID: 28560609
  8. Distinct roles for motor neuron autophagy early and late in the SOD1(G93A) mouse model of ALS. PMID: 28904095
  9. It was observed that global AQP4 expression increased in the spinal cord of SOD1G93A mice as the disease progressed. However, AQP4 polarization decreased as the disease progressed, and AQP4 polarized localization at the endfeet of astrocytes was decreased in the spinal ventral horn of SOD1G93A mice at the disease onset and end stages. PMID: 28627708
  10. Superoxide dismutase 1 mutation is associated with amyotrophic lateral sclerosis. PMID: 28019127
  11. Restrictive Lung Disease in the Cu/Zn Superoxide-Dismutase 1 G93A Amyotrophic Lateral Sclerosis Mouse Model. PMID: 28248134
  12. Endogenous MIF reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of amyotrophic lateral sclerosis. PMID: 27551074
  13. This study indicates that axonal and neuromuscular junction degeneration in the SOD1 model of amyotrophic lateral sclerosis is a complex and evolving sequence of events PMID: 27038603
  14. In this newborn mouse lung hypoxia-reoxygenation model, we found downregulation of genes of mediators of inflammation, an antiapoptotic gene expression pattern, and downregulation of DNA glycosylases. Sod1 and Il1b were significantly differentially expressed when comparing reoxygenation using 60% O2 with air. PMID: 27529351
  15. the senescence associated secretory phenotype was also increased significantly in the kidney of Sod1(-/)(-) mice compared to WT mice as measured by the expression of transcripts for IL-6 and IL-1b PMID: 27846439
  16. Our study provides the first direct evidence that Abeta, an AD-linked factor, is associated to the pathogenesis of ALS and provides molecular clues to understand common aggregation mechanisms in the pathogenesis of neurodegenerative diseases. PMID: 28864422
  17. deletion-rescue experiments show that a respiration-defective mutant of SOD1 is also impaired in its ability to rescue cells from toxicity caused by SOD1 deletion PMID: 28739857
  18. These findings indicate that a loss of Sig1R function is causative for juvenile amyotrophic lateral sclerosis (ALS16), and collapse of the mitochondria-associated membrane is a common pathomechanism in both Sig1R- and SOD1-linked ALS. PMID: 27821430
  19. the aberrant mutant SOD1-G3BP1 interaction affects stress granule dynamics PMID: 27481264
  20. the absence of IP3R2 led to increased innate immunity, which may contribute to the decreased survival of the SOD1(G93A) mice.our data indicate that IP3R2 protects against the negative effects of inflammation, suggesting that the increase in IP3R2 expression in ALS patients is a protective response. PMID: 27378687
  21. the redox regulation of Jmjd3 is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization. PMID: 26699812
  22. two ALS-linked factors, SQSTM1 and ALS2, have distinct but additive protective roles against mutant SOD1-mediated toxicity by modulating neuronal proteostasis possibly through the autophagy-endolysosomal system. PMID: 27439389
  23. we showed that, in the absence of ERalpha, G93A-SOD1 failed to activate OMI and the proteasome, confirming the ERalpha dependence of the response. Taken together, these results demonstrate the IMS-UPRmt activation in SOD1 familial Amyotrophic lateral sclerosis , and suggest that sex differences in the disease phenotype could be linked to differential activation of the ERa axis of the IMS-UPRmt PMID: 28186560
  24. The cross-sectional area of the pial arteriolar wall was increased in SOD1 deficiency, and a hyperhomocysteinemic diet sensitized SOD1-deficient mice to this hypertrophic effect. Analysis of of the vascular wall demonstrated a increase in the content of smooth muscle and elastin. We conclude that superoxide is a driver of both cerebral vascular hypertrophy and vasomotor dysfunction in a model of hyperhomocysteinemia. PMID: 28414812
  25. SOD1 has a role in amyotrophic lateral sclerosis disease phenotype PMID: 26878886
  26. the damage and satellite cell state of the gastrocnemius muscle in SOD1 knockout mice, was investigated. PMID: 26798428
  27. Events occurring locally in the skeletal muscle of SOD1 mutant mice contribute to the impairment of CaV1.1 function in ALS muscle independently of innervation status. PMID: 27340545
  28. G85R-SOD1:YFP inclusion pathology quickly spreads to discrete neurons in the brainstem and midbrain that are synaptically connected to spinal neurons PMID: 26650262
  29. SOD1 aggregates interact with the cell surface triggering activation of Rac1 and subsequent membrane ruffling permitting aggregate uptake via stimulated macropinocytosis PMID: 26520394
  30. age-related increases were mitigated by caloric restriction but not super oxide dismutase 1 overexpression PMID: 26476235
  31. postmitotic expression SOD1G93A mutant gene promotes a FAPS phenotype in C2C12 cells, by upregulating HDAC4 protein and preventing the BAF60C-SWI/SNF complex myogenic commitment PMID: 26491230
  32. The oxidative stress of diabetes mellitus impairs Wnt signaling and causes cardiac outlet defects that are rescued by SOD1 overexpression PMID: 26232087
  33. This study demonistrated that proprioceptive nerve endings in muscles revealed early and significant alterations at Ia/II proprioceptive nerve endings in muscle spindles and occur alongside those at alpha-motor axons in SOD1(G93A) mice. PMID: 26136049
  34. Mutant SOD1 Increases APP Expression and Phosphorylation in Cellular and Animal Models of ALS PMID: 26600047
  35. despite the low visceral fat in Sod1-knockout (KO) mouse, lipid droplets accumulate in the liver to a greater extent than for the wild-type mouse upon fasting PMID: 26474701
  36. Loss of SOD1 recapitulates many neuromuscular and muscle fiber changes seen in old mice. PMID: 25841780
  37. mutation is a cause of amyotrophic lateral sclerosis. PMID: 25736480
  38. Cys111 is a critical residue for the neuronal toxicity of mutant SOD1 in vivo, and the blockage of peroxidation of this residue in mutant SOD1 may constitute a future target for developing ALS treatment. PMID: 25762155
  39. Homozgous Sod1(D83G/D83G) mutant mice develop progressive degeneration of lower and upper motor neurons. PMID: 25468678
  40. Although the protein levels of the three catalytic components of the proteasome, beta1, beta2, and beta5, were not significantly altered, their proteolytic activities were decreased in the SOD1-deficient RBCs PMID: 26264915
  41. SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the amyotrophic lateral sclerosis pathology. PMID: 26221023
  42. elevation in hyperoxidized Prxs, notably Prx2 and Prx3, was observed in several organs from SOD1-deficient mice. However, a SOD1 deficiency had no impact on the wheel-running activity of the mice PMID: 26079888
  43. young adult Sod1-/- mice display reduction in skeletal muscle mass and gross alterations in neuromuscular junction. PMID: 24971750
  44. Phenotype of transgenic mice carrying a very low copy number of the mutant human G93A SOD-1 gene is associated with amyotrophic lateral sclerosis. PMID: 24945277
  45. SOD prevents thrombomodulin methionine oxidation, promotes protein C activation, and protects against arterial and venous thrombosis in mice. PMID: 26069236
  46. Studied whether NO exerts modulation of superoxide levels throughout the arterial wall and if it regulates NO-dependent inhibition of neointimal hyperplasia. In vivo, NO increased SOD-1 levels following carotid artery balloon injury in a rat model. PMID: 25460325
  47. Lipogenesis is activated by oxidative stress, which is more prominent in the case of Sod1 deficiency, and appears to participate in liver steatosis. PMID: 26116535
  48. in a SOD1(G93A) mouse model of amyotrophic lateral sclerosis, resveratrol ameliorates motor neuron degeneration PMID: 25057490
  49. exposure to either 14- or 28-day chronic stress resulted in a depressive-like syndrome, behavioural invigoration and aggression, and decreased activity of two major brain peroxidation enzymes, superoxide dismutase and catalase. PMID: 24786329
  50. Study examined the ease with which motor neuron disease can be transmitted by injecting spinal cord homogenates prepared from paralyzed mice expressing mutant superoxide dismutase 1 into the spinal cords of genetically vulnerable SOD1 transgenic mice PMID: 25262000

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