Name: SOD1 Cu/Zn - ¹⁵N
Price: 377.00 USD

- Overview
  - MW = 32.6 kDa (dimer) calculated, 32.9 kDa (metallated dimer). Human WT-SOD1 cloned from Human cDNA, expressed in E. coli. The protein consists of the full length human Cu, Zn SOD1 S-S (residues 1-154, UniProtKB accession P00441). Four additional residues, GSFT, are present at the N-term of the monomers.
    
    Available mutant
    Ala89Val
    Asp90Ala *
    Glu100Gly
    Gly93Ala *
    Gly93Arg
    Gly93Asp *
    Ile113Phe *
    Ile113Thr *
    Ile35Thr
    Leu144Phe *
    Leu148Ile
    Leu67Val
    Thr54Arg *
    Val87Met *
    Val97Met *
    *Amyotrophic lateral sclerosis (ALS) related.
    
    Labeling: 15N
    Shipping in Dry Ice: yes
    
    Please contact us at for specific academic pricing.
- Properties
  - Source
    
    Human
    
    Type
    
    Recombinant Proteins
    
    Purification
    
    > 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as single band (monomer) migrating at a molecular weight between 14.4 and 18.4 kDa. The Cu,Zn SOD1 S-S is stable as dimer. The metallation state is verified by NMR and/or mass analysis.
    
    Formulation
    
    1.0 mg/mL solution in sodium phosphate buffer 50 mM, pH 7.0. The concentration is calculated by the analysis of the absorbance at 265 nm (ε265 = 15900 M^-1cm^-1 calculated).
    
    Storage
    
    -20°C. The protein is stable at 4°C for at least 2 weeks and at 25°C for several hours. After initial defrost, aliquot the product into individual tubes and refreeze at -20°C. Avoid repeated freeze/thaw cycles.
    
    Molecular Weight
    
    32600 Da (dimer)
    
    Expression system
    
    E. coli
    
    Sequence
    
    10 20 30 40 50
    GSFT-MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE
    60 70 80 90 100
    FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI
    110 120 130 140 150
    EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI
    
    GIAQ
    
    * This product is intended for research use or further manufacturing only.
- Reference
  - Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS

SOD1 Cu/Zn - ¹⁵N

SOD1 Cu/Zn - ¹⁵N

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