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. Author manuscript; available in PMC: 2009 Oct 23.
Published in final edited form as: Neurobiol Dis. 2008 May 2;31(2):198–208. doi: 10.1016/j.nbd.2008.04.005

Figure 3.

Figure 3

Tau-nY18 antibody does not cross-react with other nitrated proteins known to undergo nitration in human diseases. Recombinant α-synuclein (A) and β-tubulin (B) proteins were exposed to either vehicle (−) or peroxynitrite (ONOO−) (+), then resolved by SDS-PAGE and probed with the indicated antibodies. Antibodies against α-synuclein and β-tubulin identify the presence of monomers in vehicle treated samples. Insoluble oligomers were detected following ONOO− treatment using 3-NT or antibodies against the native proteins. Within these experiments, Tau-nY18 did not label other nitrated proteins but did label tau nitrated at Tyr 18 (Con). In all cases, 50 ng of proteins were loaded per lane. Results are representative of five independent experiments.