Active Recombinant Human SOD1

Cat.No. : SOD1-1432H
Product Overview : Recombinant Human Superoxide Dismutase produced in E. coli. is a stable dimer of two identical subunits, non-glycosylated, containing 308 amino acid residues, two pairs of disulfide bonds and having a combined molecular mass of 31.6kDa.
Availability March 13, 2025
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Species : Human
Source : E.coli
Tag : Non
Description : Cu/Zn Human Superoxide Dismutase is a stable dimer of identical subunits with a combined molecular mass of 31.6kD. This enzyme dismutes the superoxide radical to molecular oxygen. This enzyme has been expressed in E. coli and purified using sequential chromatography steps.
Form : Lyophilized from a 0.2μm filtered solution in 50mM Phosphate buffer, pH7.4.
Bio-activity : ≥7000U/mg
Endotoxin : ≤1EU/μg, determined by the LAL method.
Purity : ≥95%, as determined by reduced SDS-PAGE Dimer ≥90%, as determined by SEC-HPLC.
Usage : FOR RESEARCH ONLY
Storage : Lyophilized samples are stable for greater than six months from date of receipt at -20 centigrade to -70 centigrade. The reconstituted samples can be stored under sterile conditions at 2-8 centigrade for one month or at -20 centigrade to -70 centigrade for three months without detectable loss of activity. Avoid repeated freeze-thaw cycles.
Reconstitution : It is recommended to reconstitute the lyophilized rHuSOD in sterile ddH2O.
Gene Name SOD1 superoxide dismutase 1, soluble [ Homo sapiens ]
Official Symbol SOD1
Synonyms ALS; SOD; ALS1; IPOA; hSod1; HEL-S-44; homodimer; superoxide dismutase [Cu-Zn]; Cu/Zn superoxide dismutase; SOD, soluble;epididymis secretory protein Li 44; indophenoloxidase A; superoxide dismutase, cystolic
Gene ID 6647
mRNA Refseq NM_000454
Protein Refseq NP_000445
MIM 147450
UniProt ID P00441
Chromosome Location 21q22.11
Pathway AGE/RAGE pathway, organism-specific biosystem; Amyotrophic lateral sclerosis (ALS), organism-specific biosystem; Detoxification of Reactive Oxygen Species, organism-specific biosystem
Function Rac GTPase binding; chaperone binding; copper ion binding

Not For Human Consumption!

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