Recombinant Human Cu/Zn Superoxide Dismutase, His (rHuCu/Zn SOD, His)
Human Cu/Zn Superoxide Dismutase (SOD) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide.
Product Specifications
Source
Escherichia coli.
Field of Research
Metabolism Research
Endotoxin
Less than 1EU/mg of rHuSOD, His as determined by LAL method.
Purity
>95% by SDS-PAGE and HPLC analyses.
Bioactivity
Fully biologically active when compared to standard. The potency per mg was tested by Pyrogallic Acid method and was found to be more than 10,000Units/mg.
Form
Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.
Molecular Weight
Approximately 20.0 kDa. a homodimer, non-glycosylated polypeptide chain containing 189 amino acids with 10 x His at the N-terminal.
Storage Conditions
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Notes
For research use only.
Applications Notes
We recommend that this vial be briefly centrifuged 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.
Preservative
Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.
AA Sequence
MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALEATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ
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