Both immunoactive Bβ1 and Bβ2 clones acquired enhanced PP2A activity (A). Cell lysates of SK-N-SH cells, Bβ1 and Bβ2 clones were probed with signal sequence-specific Bβ2 antiserum. The blots were detected with ECL system following incubation with secondary HRP-conjugated goat against rabbit antibody. The ectopic expressions of Bβ2 were detected Bβ2 (A) clones. Each blot was reprobed with glucose-6-phosphate dehydrogenase (GAPDH) antibody to confirm equal loading of the proteins. (B) The PP2A phosphatase activities of Bβ2 clones were determined by immunoprecipitating cell lysates with Bβ2 antisera as described in Materials and Methods. Characterizations of clones Bβ1#1 and Bβ1#2 (C) Cell lysates of SK-N-SH cells, Bβ1 and Bβ2 clones were probed with Bβ1 antiserum and reprobed with GAPDH antibody to confirm equal loading of the proteins. The blots were detected with ECL system. (D) The PP2A phosphatase activities of Bβ1 clones were determined by immunoprecipitating cell lysates with Bβ1 antisera as described before. The results represented fold of increase of activity relative to control of SK-N-SH with empty vector shown as average values in three individual experiments. The result represented mean values of three individual determinations; the bars standard errors in three independent experiments as conducted. *P < 0.05, significance of difference as compared with the control group.
Cheng et al. BMC Cell Biology 2009 10:91 doi:10.1186/1471-2121-10-91