Description

  • Product name

    Recombinant human Superoxide Dismutase 1 protein
    See all Superoxide Dismutase 1 proteins and peptides
  • Biological activity

    Fully biologically active when compared to standard.

    The potency per mg was determined by Pyrogallic Acid method and was found to be more than 1.0 × 104 IU/mg.

  • Purity

    > 95 % SDS-PAGE.
    > 95 % by HPLC.
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MGHHHHHHHHHHSSGHIEGRHMTYARAAARQARALEATKAVCVLKGDGPV QGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHF NPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIG RTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
    • Predicted molecular weight

      40 kDa including tags
    • Amino acids

      2 to 154
    • Tags

      His tag N-Terminus
    • Additional sequence information

      A homodimer, non-glycosylated polypeptide chain containing 2 × 189 amino acids with Met, Gly and 10 × His at N-terminus.

Specifications

Our Abpromise guarantee covers the use of ab201438 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Functional Studies

    HPLC

  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C long term. Avoid freeze / thaw cycle.

    pH: 7.40
    Constituent: 100% PBS

    0.2µm filtered

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

  • Reconstitution
    Briefly centrifuge prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

General Info

  • Alternative names

    • ALS
    • ALS1
    • Amyotrophic lateral sclerosis 1 adult
    • Cu/Zn SOD
    • Cu/Zn superoxide dismutase
    • Epididymis secretory protein Li 44
    • HEL S 44
    • Homodimer
    • hSod1
    • Indophenoloxidase A
    • IPOA
    • Mn superoxide dismutase
    • SOD
    • SOD soluble
    • SOD1
    • SOD2
    • SODC
    • SODC_HUMAN
    • Superoxide dismutase [Cu-Zn]
    • Superoxide dismutase 1
    • Superoxide dismutase 1 soluble
    • Superoxide dismutase Cu Zn
    • Superoxide dismutase cystolic
    see all
  • Function

    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
  • Involvement in disease

    Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400]. 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.
  • Sequence similarities

    Belongs to the Cu-Zn superoxide dismutase family.
  • Post-translational
    modifications

    Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal degradation.
    The ditryptophan cross-link at Trp-33 is reponsible for the non-disulfide-linked homodimerization. Such modification might only occur in extreme conditions and additional experimental evidence is required.
  • Cellular localization

    Cytoplasm. The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria.
  • Information by UniProt

References

ab201438 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab201438.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

Sign up