SOD1 / Superoxide Dismutase Antibody, Mouse MAb
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SOD1 / Superoxide Dismutase Antibody, Mouse MAb PDF Download

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Primary antibody | Secondary antibody | Tag antibody | Isotype control antibody | Loading control antibody | Antibody Purification

SOD1 / Superoxide Dismutase Antibody Datasheet

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SOD1 / Superoxide Dismutase Antibody Product Information

Immunogen :

Recombinant Human SOD1 / Superoxide Dismutase protein (Catalog#11727-H07E)

Antibody Type : Mouse Monoclonal Antibody ( Mouse mAb Service Platform )

Clone ID :


Ig Type :

Mouse IgG2b

Formulation : 0.2 μm filtered solution in PBS, 5% trehalose may be added in some batches. Please read the hardcopy of COA or contact our customer service to confirm the formulation.
Preparation :

This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human SOD1 / Superoxide Dismutase (rh SOD1 / Superoxide Dismutase; Catalog#11727-H07E; NP_000445.1; Ala 2-Gln 154).

SOD1 / Superoxide Dismutase Antibody Usage Guide

Specificity :

Human SOD1 / Superoxide Dismutase

Flow Cytometry :
SOD1 / Superoxide Dismutase Flow Cytometry

Flow cytometric analysis of Human SOD1 expression in HeLa cells. The cells were treated according to manufacturer's manual (BD Pharmingen™ Cat. No. 554714), and stained with Purified Mouse anti-SOD1 (11727-MM11, 1 μg/test), then a FITC-conjugated second step antibody. The fluorescence histograms were derived from gated events with the forward and side light-scatter characteristics of intact cells.

Flow cytometry was performed on a BD FACSCalibur flow cytometry system

Please refer to www.sinobiological.com/Flow-Cytometry-FACS-Protocols-a-750.html for technical protocols.

Storage : This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

SOD1 / Superoxide Dismutase Antibody Related Products & Topics

SOD1 / Superoxide Dismutase Antibody Related Areas:

Cancer>>Apoptosis>>Oxidative Stress>>SOD1/Cu/Zn-SOD

Enzyme>>Oxidative Stress Enzymes>>SOD1/Cu/Zn-SOD


Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
SOD1/Cu/Zn-SOD Human SOD1/Cu/Zn-SOD Protein, Recombinant 11727-H07E


Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
WB, ELISA SOD1/Cu/Zn-SOD Antibody, Rabbit MAb 11727-R101
WB, ELISA SOD1/Cu/Zn-SOD Antibody, Rabbit PAb 11727-RP01
WB, ELISA SOD1/Cu/Zn-SOD Antibody, Rabbit PAb (Antigen Affinity Purified) 11727-RP02
FCM SOD1 / Superoxide Dismutase Antibody 11727-MM11

SOD1 / Superoxide Dismutase Antibody Background

Superoxide dismutase [Cu-Zn], also known as superoxide dismutase 1 and SOD1, is an enzyme that in humans is a cytoplasm protein which belongs to theCu-Zn superoxide dismutase family. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals in the body. SOD1 is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide. SOD1 has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Death usually occurs within 2 to 5 years. The disease is inherited in 5-10% of cases leading to familial forms.


  1. Kostrzewa M. et al., 1996 Hum. Genet. 98: 48-50.
  2. Roberts B.R., et al., 2007, J. Mol. Biol. 373: 877-90.
  3. Strange R.W., et al., 2007, Proc. Natl. Acad. Sci. USA. 104: 10040-4.
  4. Cao X., et al., 2008, J. Biol. Chem. 283: 16169-16177.


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