Ue to are indicated in red and the unique exon in is indicated in green. Bars represent 1 kb and 10 kb scales for exon and intron lengths, respectively. (B) ClustalX alignment of mouse Epb4.1l5and zebrafish Moe. Ymo1and Moe share a high degree of homology within the FERM domain (black). Ymo1and Ymo1are identical up to Lysine 444 (blue arrow) and then alternately spliced into the long (red) and short (green) isoforms. Moe and Epb4.1l5, and Epb4.1l5have predicted C'terminal PDZ-binding domains (Pink [TTEL]) and (light green [MTEI]). (*) identical, (:) highly conserved, (.) moderately conserved. (C) Western analysis of mouse tissues with antibodies raised against the unique C'terminal sequences of Epb4.1l5and Epb4.1l5. Two bands are immunoreactive with the anti-Epb4.1l5antibody, one migrates at the expected molecular weight of Epb4.1l5(100 kDa) and is present in the eye, brain, heart, lung, kidney, and testis. An additional band migrates at 75 kDa, which is probably non-specific. Two bands are recognized by the affinity purified Epb4.1l5antibody. A lower band migrates at the predicted molecular weight of 56 kDa and is present in brain, liver, lung, kidney, pancreas, and gut. A second band with a broad expression pattern migrates at approximately 75 kDa. Anti-α-Tubulin was used as a loading control.Copyright information:Taken from "Tissue-specific requirements for specific domains in the FERM protein Moe/Epb4.1l5 during early zebrafish development"http://www.biomedcentral.com/1471-213X/8/3BMC Developmental Biology 2008;8():3-3.Published online 11 Jan 2008PMCID:PMC2266719.