Rabbit IgG polyclonal antibody for Superoxide dismutase [Cu-Zn] (SOD1) detection. Tested with WB, IHC-P, IHC-F, ICC in Human, Mouse, Rat.
Immunogène
A synthetic peptide corresponding to a sequence at the C-terminal of Human SOD, different from the mouse sequence by two amino acids.< br/>Immunogen was affinity purified.
At -20 °C for one year. After reconstitution, at 4 °C for one month. It can also be aliquotted and stored frozen at -20 °C for a longer time.
Crapo, Oury, Rabouille, Slot, Chang: "Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 21, pp. 10405-9, (1992) (PubMed).
Superoxide dismutases (SOD) are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism. Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.