Fig. 2. In vitro transcription/translation of AeaEAAT and western analysis. In vitro transcription and translation of the AeaEAAT cDNA produces a translation product that migrates at approximately 40 kDa on an 8% SDS-PAGE gel (lane 1). AeaEAAT is expressed in both the head of the adult Ae. aegypti (lane 2), as well as in Xenopus laevis oocytes injected with the cRNA encoding AeaEAAT as a protein (lane 4) with mobility of 55 kDa. Membranes prepared from the whole head of adult Ae. aegypti and from Xenopus laevis oocytes expressing AeaEAAT were separated by 8% SDS-PAGE, transferred to Immobilon P (Millipore), and subjected to western analysis, using the affinity-purified -AeaEAT antibody. Preincubation of the primary antibody with the antigenic peptide abolished any signal. Lanes 2 and 5, adult Ae. aegypti head membranes; lanes 3 and 6, Xenopus laevis oocytes injected with cRNA of a Drosophila sodium channel; lanes 4 and 7, X. laevis oocytes injected with cRNA of pBSAMVBC10. Note that lanes 5–7 are probed with the primary antibody upon preadsorption with the antigenic peptide. The positions of molecular mass (kDa) proteins are shown.