Figure 4From: Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiationDetection of Par17 in cell lysates. A. Western blot of HeLa and HepG2 cell lysates. 10 and 50 μg HeLa (lane 1 and 2) and 10 and 50 μg HepG2 (lane 3 and 4) cell extracts were separated by SDS-PAGE with Tris-glycine as running buffer and transferred to nitrocellulose membranes. SeeBlue2 was used as protein standard. Blots were incubated with Ab-PPIase (polyclonal antibody against Parvulin's PPIase domain as described [11,12], stripped by 2% SDS at 65°C and re-probed with affinity purified Ab-EXT (against the N-terminal extension). Coomassie stained membrane is shown as loading control. B. Fresh protein samples (lane 1) as well as samples subjected to repeated freeze-thaw cycles (lane 2) were analyzed by Western blots using anti-Par17 antiserum. C; HeLa cell extracts were separated by SDS-PAGE with Tris-glycine as running buffer, transferred to nitrocellulose and incubated with antibodies against SUMO-1 (lane1), SUMO-2/3 (lane2) and Ubiquitin (lane3). Magic Mark was used as protein standard.Back to article page