Anti stathmin

Western blot was employed to disclose the expression status of proteins according to a method previously described [33 (link)] (anti- stathmin 1:800; anti- MMP2 1:1000, Abcam Company; anti- p38 MAPK 1:1000, Abcam Company; Phospho-p38 MAPK Antibody 1:1000, BioVision Inc.). We used β-actin as the internal control.

Immunoblotting was performed as previously described [9 (link)]. In brief, whole protein lysates were separated by SDS/PAGE and transferred to nitrocellulose membranes (Whatman, Dassel, Germany). Membranes were incubated with the following primary antibodies diluted in 5% Milk/TBST-containing blocking solution overnight: anti-KPNA2 (rabbit polyclonal, 1:2000; abcam, Cambridge, UK), anti-stathmin (rabbit monoclonal, 1:1000; abcam), anti-E2F1 (rabbit polyclonal, 1:200; Santa Cruz, Heidelberg, Germany), anti-TFDP1 (rabbit polyclonal, 1:500; abcam), anti-ATF-2 (rabbit polyclonal, 1:200; Santa Cruz), anti-FBP-1/2 (goat polyclonal, 1:200; Santa Cruz), anti-c-JUN (rabbit monoclonal, 1:2000; Cell Signaling Technology, Frankfurt, Germany), anti-HMOX1 (rabbit monoclonal, 1:10,000; abcam), anti-GTSF1 (goat polyclonal, 1:200; Santa Cruz), anti-PARP (rabbit polyclonal, 1:500; Cell Signaling Technology), anti-β-tubulin (mouse monoclonal, 1:1000; Becton, Dickinson and Company, Franklin Lakes, USA) and anti-β-actin (mouse monoclonal, 1:10,000; MP Biomedicals, Illkirch, France). Blots were incubated with fluorescence-conjugated secondary antibodies (LI-COR Bioscience, Bad Homburg, Germany) for one hour and detection was performed using the Odysee Sa Infrared Imaging System (LI-COR Bioscience).