The apicomplexan parasite Plasmodium falciparum is the causative agent of malaria and is responsible for >400,000 deaths per year, mainly of children under the age of five. The onset of drug resistance against our frontline antimalarials is becoming a significant threat and is further exacerbated by the lack of an effective licensed vaccine. We must therefore prioritize the identification of novel proteins which are targetable by new vaccines. In pursuit of this, we have have begun detailed functional characterisation of a zinc-finger protein of P. falciparum (Pf3D7_1468400) which is expressed during the invasive merozoite stage of the parasite lifecycle. Pf3D7_1468400 is highly conserved across P. falciparum isolates, has previously been localised to the merozoite surface and was reported to be susceptible to growth inhibitory vaccine induced antibodies; characteristics typical of leading vaccine candidates. Using gene editing approaches, our knock-out and knock-down parasite models demonstrated that Pf3D7_1468400’s role in red blood cell invasion and blood stage growth is not essential. We explored Pf3D7_1468400’s cellular localization in the merozoite using biochemical assays which indicated that the protein was unlikely to be on the merozoite surface, in contrast to the findings of the earlier study. Immunofluorescence microscopy studies are ongoing to determine Pf3D7_1468400’s accessibility to antibodies, however the protein’s limited signal has made it difficult to confirm its localisation within the merozoite. This study is the first detailed attempt to determine the function of the zinc-finger protein Pf3D7_1468400, with early results calling into questions its suitability as a vaccine target.