Abstract
The Drosophila glypican Dally-like protein (Dlp) is an evolutionarily-conserved cell-surface protein that modulates extracellular distribution of several secreted ligands for cell signaling. Several fly lines expressing tagged dlp have been used to study the role of Dlp in vivo including the PBac{602.P.SVS-1}dlp [CPTI000445] protein-trap line, which encodes StrepII-Venus-StrepII (SVS)-tagged Dlp from the endogenous locus. dlp is essential for embryonic development, and the SVS-dlp line is homozygous viable. Although this suggests that the SVS-tagged Dlp is functional, it is possible that that the SVS-dlp flies produce wild-type dlp isoform through alternative splicing, contributing to their survival. Here, we used a molecular analysis approach to show that the SVS-dlp flies do not produce wild-type isoform, confirming that the SVS-tagged Dlp is indeed functional.