This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 16.8 kDa. The protein migrates as 20 kDa under reducing (R) condition (SDS-PAGE).
SOD1
Spezies: Schwein
Wirt: Escherichia coli (E. coli)
Recombinant
> 97 %
WB, SDS, Imm, PC
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
50 mM Tris, 150 mM NaCl, pH 7.5
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Sakanyan, Hulin, Alves de Sousa, Silva, Hambardzumyan, Nedellec, Tomasoni, Logé, Pineau, Roussakis, Fleury, Artaud: "Activation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1." in: Scientific reports, Vol. 6, pp. 21088, (2016) (PubMed).
Superoxide dismutase [Cu-Zn] (SOD1) is also known as superoxide dismutase 1 (hSod1), an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 can bind copper and zinc ions and is one of three superoxide dismutases responsible for destroying free superoxide radicals in the body. The encoded isozyme (SOD1) is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide. Furthermore, the mutations of SOD1 gene can result in a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord.