Recombinant :
Recombinant Human Cu/Zn Superoxide Dismutase, His (rHuCu/Zn SOD, His ) Source :
Escherichia coli. Molecular Weight :
Approximately 20.0 kDa. a homodimer, non-glycosylated polypeptide chain containing 189 amino acids with 10 x His at the N-terminal. Purity :
>95% by SDS-PAGE and HPLC analyses. Biological Activity :
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. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
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 Endotoxin :
Less than 1EU/mg of rHuSOD, His as determined by LAL method. Reconstitution :
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. Storage :
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. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China Description :
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.
Recombinant Human Cu/Zn Superoxide Dismutase, His (rHuCu/Zn SOD, His ) Source :
Escherichia coli. Molecular Weight :
Approximately 20.0 kDa. a homodimer, non-glycosylated polypeptide chain containing 189 amino acids with 10 x His at the N-terminal. Purity :
>95% by SDS-PAGE and HPLC analyses. Biological Activity :
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. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
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 Endotoxin :
Less than 1EU/mg of rHuSOD, His as determined by LAL method. Reconstitution :
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. Storage :
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. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China Description :
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.
Blocking peptide available as PR1013P