Western Blot: SOD1/Cu-Zn SOD Antibody [NBP1-31204] - Non-transfected (-) and transfected (+) 293T whole cell extracts (30 ug) were separated by 15% SDS-PAGE, and the membrane was blotted with SOD1 antibody.
Immunocytochemistry/ Immunofluorescence: SOD1/Cu-Zn SOD Antibody [NBP1-31204] - HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: SOD1 protein stained by SOD1 antibody (NBP1-31204) diluted at ...read more
Immunohistochemistry-Paraffin: SOD1/Cu-Zn SOD Antibody [NBP1-31204] - Paraffin-embedded Muscle, using antibody at 1:500 dilution. (Mouse)
Western Blot: SOD1/Cu-Zn SOD Antibody [NBP1-31204] - Sample (50 ug of whole cell lysate) A: Rat brain 15% SDS PAGE; antibody diluted at 1:1000.
Western Blot: SOD1/Cu-Zn SOD Antibody [NBP1-31204] - Analysis of SOD1 and beta-actin (lower panel) Sample (30 ug of whole cell lysate) A: HeLa mock control B: HeLa transfected shSOD1 15% SDS PAGE.
16 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read 1 Review rated 5 using NBP1-31204 in the following applications:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD1), mitochondrial manganese SOD (Mn-SOD/SOD2) and extracellular Cu, Zn-SOD (EC-SOD/SOD3). SOD1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80-kDa tetrameric enzyme SOD2 is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin binding multimer of disulfide linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase(CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Sample Information: Treatment: None. Run on control tissue Controls: Positive Control: None Negative Control: Primary only, secondary only, and secondary with IgG all negative Loading Control: Ponceau S stain
Total Protein Loaded: 40 ug/well
Electrophoresis: Gel Percentage: Gradient, 4-20% Electrophoresis Conditions: Voltage: 50V then 90V Time: 5 min then 1 hr
Membrane Transfer: Method (Submersion/Semi-dry): Semi-dry using iBlot2 system Membrane Type (PVDF/Nitrocellulose): Nitrocellulose Time: 7 min (iBlot2 Protocol 0)
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