Antisera, raised against Drosophila huntingtin, detected increased signals in the nucleus of S2 cells with nuclear dorsal accumulation after LPS treatment. a,b, Western blot analysis was performed using transfected and non-transfected S2 cells. Full-length and amino-terminal fragment of Drosophila huntingtin were expressed by Gal4-UAS system  using pUAS-DhdcDNA (lanes 3 and 5), pUAS-Dhdminigene (lane 7), pUAS-N605 (lanes 1 and 6), and actin5C-Gal4. Antisera 1893 ( a ) and 1894 ( b ), raised against the amino-terminal region of Drosophila huntingtin, recognized the products of the transgenes (arrow: full-length huntingtin, and arrow head: N605), and also detected an approximately 400kDa native protein corresponding to over-expressed full-length Drosophila huntingtin in size which is thought to be native Drosophila huntingtin. c, Antiserum 1894 recognized mainly cytoplasmic immunoreactivity with minor nuclear signals. Transfected NLS-GFP-lacZ detected by anti-lacZ antibody and Alexa Fluor 488 goat anti-mouse IgG was used for a control nuclear maker. d, Antiserum1894 recognized apparent nuclear immunoreactivity, when FLAG-Dorsal was accumulated in the nucleus after LPS treatment. FLAG-Dorsal was detected by anti-FLAG M5 antibody and Alexa Fluor 488 goat anti-mouse IgG.