Figure 7
Oligomerization of AKAP5 expressed and purified from E. coil : analysis of higher-order assembly by steric-exclusion chromatography. His-tagged AKAP5 was expressed in E. coli. The AKAP5 was purified and then resolved by steric-exclusion chromatography performed on an AKTA FPLC fitted with HiPrep Sephacryl-S400 (16/60) column. The presence of supermolecular oligomers of AKAP5 was established by SDS-PAGE and immunoblotting of samples from the chromatography. The resolved, transferred proteins were stained with anti-AKAP5 antibodies. Marker protein mobilities were employed to establish the M r of AKAP5 by elution position (inset). The results displayed are representative of two separate experiments performed on as many separate cell cultures.