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. 2012 Nov 5;4:e5035add8caff4. [Version 1] doi: 10.1371/5035add8caff4

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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Pull-down assay of dysferlin C2A-GST and MG53. — COS-7 cells overexpressing FLAG-tagged MG53 were lysed and supplemented with DTT or NEM, and proteins in these lysates were cross-linked with GA. Cross-linked proteins were incubated with glutathione Sepharose 4B beads bound to wild-type C2A-GST, V67D C2A-GST, or GST. GST fusion proteins bound to beads were separated by SDS-PAGE, followed by Coomassie Brilliant Blue R-250-staining. Precipitated MG53 oligomers/monomers were detected on immunoblots using an anti-FLAG antibody. Mutations in the C2A domain affect the association of between dysferlin and MG53.