Recombinant Human Superoxide Dismutase His Tag

Recombinant Human Superoxide Dismutase His Tag

Catalog Number:
P001414137ABE
Mfr. No.:
Abe32-4918
Price:
  • Size:
    100 µg
    Quantity:
    Add to Cart:
      • Overview
        • SOD Human Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 189 amino acids with a 10 × His at N-terminus and having a molecular mass of 40.0kDa. The SOD Human is purified by proprietary chromatographic techniques. Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

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      • Properties
        • Protein Name
          Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
          Source
          E. coli
          Type
          Recombinant Proteins
          Purification
          Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
          Formulation
          Lyophilized from a 0.2um filtered concentrated solution in PBS, pH 7.4.
          Storage
          Lyophilized SOD Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SOD Human should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

      • Applications
        • Application Description
          It is recommended to reconstitute the lyophilized SOD in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Fully biologically active when compared to standard. The specific activity was tested by Pyrogallic Acid method and was found to be more than 10,000Units/mg.

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