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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

Available Sizes

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