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Human SOD1 / Superoxide Dismutase ELISA Pair Set

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Materials provided
Capture Ab:0.2 mg/mL of mouse anti-SOD1 monoclonal antibody (in PBS, pH 7.4). Dilute to a working concentration of 2 μg/mL in CBS before coating.
Detection Ab:0.2 mg/mL rabbit anti-SOD1 polyclonal antibody conjugated to horseradish-peroxidase (HRP) (in PBS, 50 % HRP-Protector, pH 7.4). Dilute to working concentration of 0.25 μg/mL in detection antibody dilution buffer before use.
Standard:Each vial contains 180 ng of recombinant SOD1. Reconstitute with 1 mL detection antibody dilution buffer. After reconstitution, store at -20℃ to -80℃ in a manual defrost freezer. A seven-point standard curve using 2-fold serial dilutions in sample dilution buffer, and a high standard of 4 ng/mL is recommended.
The minimum detectable dose of Human SOD1 / Superoxide Dismutase was determined to be approximately 62.5 pg/ml. This is defined as at least three times standard deviations above the mean optical density of 10 replicates of the zero standard.
Principle of the product
The Human SOD1 / Superoxide Dismutase ELISA Pair Set is for the quantitative determination of Human SOD1 / Superoxide Dismutase.
This ELISA Pair Set contains the basic components required for the development of sandwich ELISAs.
The Sino Biological ELISA Pair Set is a solid phase sandwich ELISA (Enzyme-Linked Immunosorbent Assay). It utilizes a monoclonal antibody specific for SOD1 / Superoxide Dismutase coated on a 96-well plate. Standards and samples are added to the wells, and any SOD1 / Superoxide Dismutase present binds to the immobilized antibody. The wells are washed and a horseradish peroxidase conjugated rabbit anti-SOD1 / Superoxide Dismutase polyclonal antibody is then added, producing an antibody-antigen-antibody "sandwich". The wells are again washed and TMB substrate solution is loaded, which produces color in proportion to the amount of SOD1 / Superoxide Dismutase present in the sample. To end the enzyme reaction, the stop solution is added and absorbances of the microwell are read at 450 nm.
Capture Antibody: Aliquot and store at -20℃ to -80℃ for up to 6 months from date of receipt. Avoid repeated freeze-thaw cycles.
Detection Antibody: Store at 4℃ and protect it from prolonged exposure to light for up to 6 months from date of receipt. DO NOT FREEZE!
Standard: Store lyophilized Standard at -20℃ to -80℃ for up to 6 months from date of receipt. Aliquot and store the reconstituted Standard at -80℃ for up to 1 month. Avoid repeated freeze-thaw cycles.

SOD1 belongs to the Cu-Zn superoxide dismutase family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.

  • Murakami K, et al. (2011) SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. J Biol Chem. 286(52):44557-68.
  • Thompson M, et al. (2012) Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis. J Neurochem. 120(4):598-610.
  • Magrané J, et al. (2012) Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J Neurosci. 32(1):229-42.
  • Gertz B, et al. (2012) Nuclear localization of human SOD1 and mutant SOD1-specific disruption of survival motor neuron protein complex in transgenic amyotrophic lateral sclerosis mice. J Neuropathol Exp Neurol. 71(2):162-77.
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