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. Author manuscript; available in PMC: 2015 Feb 20.
Published in final edited form as: J Cell Sci. 2012 Mar 7;125(0 4):1048–1057. doi: 10.1242/jcs.098392

Fig. 3. Co-precipitates of BAF and Ankle1 in vitro.

Fig. 3

(A) BAF-6xHis was mixed with E.coli lysates containing recombinant Ankle1, Ankle1ΔCT or an N-terminal Emerin fragment EmerinΔTM and precipitated usining Ni-beads. BAF-bound proteins were detected by Western blotting using antiserum ‘136′ (Ankle1), India His-probe (BAF) and monoclonal antibody ‘MANEM5’ to emerin (gift of Glenn Morris). S, supernatant fraction (10% of input); P, precipitated fraction (50% of preciptated proteins). Molecular weights are indicated in kDa. The scheme shows the Ankle1 constructs used in the assays. (B) Recombinant 6xHis-V5 tagged Ankle1, Ankle1b or LAP2α were incubated with bacterial lysates containing untagged human BAF. His-tagged prey proteins were precipitated using Ni-beads and bound BAF was detected by Western blotting using antibodies to V5 tag and BAF. S, supernatant fraction (10% of input); P, precipitated fraction (50% of preciptated proteins). Note: BAF forms various homomeric complexes even under denaturating conditions (arrows indicating monomeric, dimeric and oligomeric states).