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. 2016 Jul 25;9:413. doi: 10.1186/s13071-016-1695-y

Fig. 5.

Fig. 5

Recombinant Lulo protein has a molecular weight around 40–45 kDa and is recognized by anti-rLulo antibodies. The recombinant Lulo protein was purified by affinity chromatography with lectin from Helix pomatia (HPA). Eluent together with lysate of Lu. longipalpis midguts was analyzed by SDS-PAGE, followed by western blot with anti-rLuloG antibodies. Antibodies against rLuloG recognized one molecule in fraction eluted with N-acetyl-galactosamine (GalNAc), which has molecular weight around 40–45 kDa (Lane 1). Preimunne serum was used as a control, which did not recognize any molecules in fraction eluted with GalNAc (Lane 1c). The recombinant molecule was labeled also with HPA (Lane 2) and the reaction was inhibited by specific GalNAc (Lane 2c). Anti-rLulo serum recognized also the native molecule in a midgut lysate of Lu. longipalpis (Line 3), preimunne serum did not react with the Lu. longipalpis midgut lysate (Lane 3c)