Cu/Zn Superoxide Dismutase Monomer
Human Recombinant SOD1
Reference ID:KB-1811
Western Blot
Gene of Interest
Gene Synonyms:SOD1
Protein Names:Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (hSod1)
Accession Data
Organism:Homo sapiens (Human)
Mass (kDa):159.36
Length (aa):154
Sequence:MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Proteomics (Proteome ID):UP000005640
Proteomics (Chromosome): Chromosome 21
Catalytic Activity: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
Cofactor:Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:17888947}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:17888947}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17888947}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17888947};
Function [CC]:Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Metal Binding:METAL 47 47 Copper; catalytic. {ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825}.; METAL 49 49 Copper; catalytic. {ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825}.; METAL 64 64 Copper; catalytic. {ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825}.; METAL 64 64 Zinc; via pros nitrogen. {ECO:0000269|PubMed:20727846}.; METAL 72 72 Zinc; via pros nitrogen. {ECO:0000269|PubMed:20727846}.; METAL 81 81 Zinc; via pros nitrogen. {ECO:0000269|PubMed:20727846}.; METAL 84 84 Zinc; structural. {ECO:0000269|PubMed:20727846}.; METAL 121 121 Copper; catalytic. {ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825}.
Chemical Profile | ChEBI:H2O2 [CHEBI:16240]; Zn(2+) [CHEBI:29105]; H(+) [CHEBI:15378]; Cu cation [CHEBI:23378]; O2 [CHEBI:15379]; superoxide [CHEBI:18421]
ChEBI (Catalytic Activity):H2O2 [CHEBI:16240]; H(+) [CHEBI:15378]; O2 [CHEBI:15379]; superoxide [CHEBI:18421]
ChEBI (Cofactor):Zn(2+) [CHEBI:29105]; Cu cation [CHEBI:23378]
Disease:Amyotrophic lateral sclerosis 1 (ALS1) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. 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 the cases. {ECO:0000269|PubMed:10400992, ECO:0000269|PubMed:10430435, ECO:0000269|PubMed:10732812, ECO:0000269|PubMed:11369193, ECO:0000269|PubMed:11535232, ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12402272, ECO:0000269|PubMed:12754496, ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:14506936, ECO:0000269|PubMed:15056757, ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:18378676, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21247266, ECO:0000269|PubMed:27604643, ECO:0000269|PubMed:7496169, ECO:0000269|PubMed:7501156, ECO:0000269|PubMed:7647793, ECO:0000269|PubMed:7655468, ECO:0000269|PubMed:7655469, ECO:0000269|PubMed:7655471, ECO:0000269|PubMed:7700376, ECO:0000269|PubMed:7795609, ECO:0000269|PubMed:7836951, ECO:0000269|PubMed:7870076, ECO:0000269|PubMed:7881433, ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7951252, ECO:0000269|PubMed:7980516, ECO:0000269|PubMed:7997024, ECO:0000269|PubMed:8069312, ECO:0000269|PubMed:8179602, ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, ECO:0000269|PubMed:8528216, ECO:0000269|PubMed:8682505, ECO:0000269|PubMed:8907321, ECO:0000269|PubMed:8938700, ECO:0000269|PubMed:8990014, ECO:0000269|PubMed:9101297, ECO:0000269|PubMed:9131652, ECO:0000269|PubMed:9455977, ECO:0000269|PubMed:9541385}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Mutagenesis:MUTAGEN 7 7 C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:22496122}.; MUTAGEN 7 7 C->S: No palmitoylation, reduced nuclear targeting. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:22496122}.; MUTAGEN 51 52 FG->EE: Abolishes dimerization; when associated with Q-134. {ECO:0000269|PubMed:10329151, ECO:0000269|PubMed:18552350}.; MUTAGEN 58 58 C->A: Exhibits very slow copper acquisition. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804}.; MUTAGEN 58 58 C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804}.; MUTAGEN 81 81 H->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. {ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350}.; MUTAGEN 81 81 H->S: Destabilization of dimer and loss of zinc binding; when associated with S-84. {ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350}.; MUTAGEN 84 84 D->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. {ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350}.; MUTAGEN 84 84 D->S: Destabilization of dimer and loss of zinc binding; when associated with S-81. {ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:18552350}.; MUTAGEN 112 112 C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350}.; MUTAGEN 123 123 K->A: Deacreased succinylation. {ECO:0000269|PubMed:24140062}.; MUTAGEN 123 123 K->E: Mimicks constitutive succinylation state; decreased activity. {ECO:0000269|PubMed:24140062}.; MUTAGEN 134 134 E->Q: Abolishes dimerization; when associated with E-50 and E-51. {ECO:0000269|PubMed:10329151}.; MUTAGEN 147 147 C->A: Exhibits very slow copper acquisition. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804}.; MUTAGEN 147 147 C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. {ECO:0000269|PubMed:17070542, ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804}.
Miscellaneous [CC]:The protein (both wild-type and ALS1 variants) 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.
Reagent Data
Name:Cu/Zn Superoxide Dismutase Monomer
Class:Superoxide Dismutase
Subcategory:Enzyme
Molecular Weight:15.9
Source:E.Coli
Species:Human
Tag:
Amino Acid Sequence:MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ
Bioactivity
EC50=> 90 units/mg
Format:Solution
Purification System:Chromatography
Formulation:Sterile-filtered colorless solution
Formulation Concentration:1 mg/ml
Buffer Volume:20 mM
Buffer Solution: Tris-HCl
pH:7.5
Stabilizers
Glycerol:0.1
Purity:> 95%
Determined: SDS-PAGE
Sample Handling
Storage:4°C
Stability:This bioreagent is stable at 4°C (short-term) and -70°C(long-term). After reconstitution, sample may be stored at 4°C for 2-7 days and below -18°C for future use.
Preparation:Reconstitute in sterile distilled H2O to no less than 100 ug/ml; dilute reconstituted stock further in other aqueous solutions if needed. Please review COA for lot-specific instructions. Final measurements should be determined by the end-user for optimal performance.