Fig. 1

Anti-SOD1^olig antibody recognizes soluble SOD1 oligomers with the disulfide crosslinks but not folded SOD1 in vitro. (a) Description of SOD1 in distinct metallation and thiol-disulfide states. E,Zn-SOD1^S-S, in which SOD1 with the disulfide bond binds a zinc ion at the Zn-binding site, is shown as an example. (b) Specificity of purified anti-SOD1^olig antibody was examined by indirect ELISA using E,E-SOD1^S-S proteins (WT, A4V, G37R) and soluble disulfide-crosslinked oligomers (A4V, G37R). (c) No statistically significant difference in the amounts of SOD1 proteins adsorbed on wells was confirmed by ELISA using anti-SOD1 antibody (FL-154, Santa Cruz Biotechnology). The ELISA signal was represented as a ratio against that obtained using bovine serum albumin (BSA). Three independent experiments were performed to estimate error bars (standard deviation)