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https://www.selleckchem.com/pharmacological_epigenetics.html Periplasmic expression of recombinant proteins ensures the production of biologically active proteins in a correctly folded state with several key advantages. This research focused on the in-frame cloning of rhIL-15 in pET-20 (+) vector with pelB-leader sequence to direct the protein to the bacterial periplasm. The target construct periplasmic expression was evaluated in four strains, BL21 (DE3), BL21 (DE3) pLysS, Rosetta 2 (DE3) and Rosetta-gami 2 (DE3). Soluble periplasmic expression of IL-15 was highest in Rosetta-gami 2 (DE3) followed by Rossetta 2 (DE3) whereas negligible expression was observed with rest of two expression host. Best expression clone was selected for purification by dye ligand affinity chromatography. Purified rhIL-15 was characterized by SDS-PAGE, Western blotting and SEC-HPLC. This is the first report of functional recombinant human interleukin-15 being expressed and purified with yield of 120 mg/L in the periplasmic space of E. coli.The moult cycle is arguably the most critical aspect of crustacean biology and is associated with dramatic changes in behaviour, physiology and condition. Here we describe the first detailed investigation of the combined changes in morphology, physiological status and nutritional condition over the moult cycle of juvenile T. australiensis. Haemolymph refractive index (measured as Brix) was evaluated as a non-destructive method for predicting physiological status and nutritional condition. Post-moult, inter-moult and pre-moult stages were identifiable by microscopic examination of the pleopod distal tips, though differentiation of the pre-moult substages was not possible using this technique. Monitoring of ecdysial suture lines on the exoskeleton gill chambers was found to be highly useful for visually determining progression through the pre-moult stage and predicting the timing of ecdysis. A classical pattern of inter-moult growth was observed where siz

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