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Fig. 5 | Molecular Neurodegeneration

Fig. 5

From: α-synuclein interacts with SOD1 and promotes its oligomerization

Fig. 5

Pathological G85R and G93A mutations in SOD1 alter binding affinity to α-synuclein. a Immunoprecipitation of G85R and G93A SOD1-myc of co-transfected H4 cells using anti-myc antibody increasingly precipitated α-synuclein. Input: 5 μg protein. Experiment was repeated 4 times and showed similar results. b Quantification of SOD1-myc immunoprecipitations. Co-immunoprecipitated α-synuclein was normalized to immunoprecipitated wt, G85R and G93ASOD1-myc respectively. α-synuclein of input was normalized to β-actin of input (two tailed, unpaired student’s t-test, n = 3, n.s. = not significant, * p < 0,05). c α-synuclein immunoprecipitation of co-transfected H4 cells co-immunoprecipitated particularly G85R and G93A SOD1-myc. Input: 5 μg protein. Experiment was repeated 2 times with similar results. light chain = light chain of IgGs

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