SOD and mutants

Superoxide dismutase and mutants

Human WT-SOD1 cloned from human cDNA, expressed in E. coli, also available with a variety of mutations and some ALS-related mutations. Also available labeled with stable isotopes (2H/13C/15N). Quality control through mass spectrometry and NMR. Usage: SDS-PAGE, WB, ELISA, antibody production. Custom isotopic labeling available.


SOD1 Cu/Zn

Human, recombinant.
full lenght, swissprot accession P23297
MW = 32600 Da. (dimer)
EC # 1.15.1.1.
CAT # G06SD001

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G06SD001 none 0.1 mg 160.00
G06SD001 none 0.5 mg 495.00
G06SD001 none 1 mg 800.00
G06SD001 none 5 mg 2,475.00

Labeled Protein
Catalog n° Labeling Q.ty Price (€)
G06SD001n 15N 5 mg 2,860.00
G06SD001n 15N 10 mg 4,645.00
G06SD001cn 13C15N 5 mg 3,400.00
G06SD001cn 13C15N 10 mg 5,525.00


Special prices for bulk quantities available upon request.

Description
MW = 32.6 kDa (dimer). Human WT-SOD1 cloned from Human cDNA, expressed in E. coli. The protein consists of the full length human Cu, Zn SOD1S-S (the mass of the metallated enzyme is 32.9 kDa) N-term end of the protein contains 4 additional aminoacids (GSFT).

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 
Purity
> 95% by SDS-PAGE. The Cu,Zn SOD1 S-S is stable as dimer. The metallation state is verified by mass analysis.

Storage
-20°C. The protein is stable at 4°C for several months and at 25°C for at least two weeks. After initial defrost, aliquot protein into individual tubes and refreeze at -20°C.
Avoid repeated freeze/defrost cycles.

References
Banci L., et. al. Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11263-7.
Banci L., et. al. J Biol Chem. 2006 Jan 27;281(4):2333-7.
Arnesano F., et. al. J Biol Chem. 2004 Nov 12;279(46):47998-8003. Epub 2004 Aug 23.

SOD1 MUTANTS AND ALS-RELATED MUTANTS

Mutants available:
  • Ala89Val
  • Asp90Ala *
  • Glu100Gly
  • Gly93Ala *
  • Gly93Arg
  • Gly93Asp *
  • Ile113Phe *
  • Ile113Thr *
  • Ile35Thr
  • Leu144Phe *
  • Leu148Ile
  • Leu67Val
  • Thr54Arg *
  • Val87Met *
  • Val97Met *
*Amyotrophic lateral sclerosis (ALS) related

Prices available upon request.

References