If no SUMOylation is found, then a heterologous co-expression of SUMO-1 and SERCA2 should be considered. With regard to the solubilisation detergent, as tested in the case of the hSERCA2a-GFP-His8 construct, no increase in the yield of purified protein was observed when using a smaller detergent: total membrane protein ratio. Thus, it can be concluded that the initial 3:1 ratio used did not contribute to the high aggregation observed during SEC. Further, based on the result obtained with FC12, it may be that usage of a higher solubility capacity detergent may lead to aggregated fraction solubilisation rather than the solubilisation of the active form of the protein. Further work would be necessary to more fully understand the effect of different detergents or lipids on human cardiac Ca2+-ATPase stability. Purified hSERCA2a showed calcium-dependent and thapsigargin-sensitive activity. The calcium K0.5 for hSERCA2a of 0.6 ��M found herein is within previously reported values. A significant difference observed in the turn-over rate between previously purified samples of SERCA2a may be explained by the different lipid content, since previous data were measured on vesicular microsomes which contain some natural lipids associated with SERCA2, whereas SERCA2a purified from S. cerevisiae was not reconstituted into liposomes and was analysed in the presence of detergent. Another plausible explanation for the differences in turn-over rate could be the presence of inactive protein in the final purified sample. Finally and importantly, are the diversity of ATPase assay conditions, which may explain the significant differences in the enzymatic activities reported. It is noteworthy that, although the turn-over rate for hSERCA2a was different than when expressed using other systems, the values obtained here are very close to the specific enzymatic activities obtained for rSERCA1a expressed and purified from S. cerevisiae. The optimised protocol Niltubacin side effects outlined in this work is easily extended to other SERCA isoforms and useful for the production of high quality recombinant active protein for further analysis to study interactions between SERCAs and their physiologically relevant partners. The resulting protein is suitable for crystallisation trials and subsequent structural analysis. Furthermore, the method outlined may prove useful generally for the recombinant production of other multi-domain eukaryotic membrane proteins. The etiological agents of human malaria are vector-borne protozoan parasites that initially infect liver cells but rapidly develop to invade and reproduce in host erythrocytes. These blood-stage parasites produce a number of proteins that are exported to the surface of the infected red blood cell. The pattern of adherence is selective in that most sequestered infected iRBCs are found in the lungs, adipose tissue, brain and placenta. The ability to sequester in the vasculature of certain tissues is thought to be advantageous to the parasite because it diminishes clearance of trophozoite- and schizont-containing iRBCs in the spleen and promotes factors that are beneficial for parasite growth. Sequestration in organs such as the lung is not without consequences, as large numbers of iRBCs in the lung have been hypothesized to precipitate events that result in lung injury. Work with synchronized PbA infections has demonstrated that schizontcontaining RBCs selectively adhere to lung microvascular endothelial cells and this interaction is dependent on capillary endothelial cell expression of CD36. Interestingly, the PbA genome does not contain any PfEMP1 orthologues. Recently, it has been demonstrated that the schizont membraneassociated cytoadherence protein is critical for PbA schizont-stage parasites to adhere to vascular Torin 1 endothelium via CD36.