Juvenile hormone (JH) plays vital roles in insect reproduction, development, and in many aspects of physiology. JH primarily acts at the gene-regulatory level through interaction with an intracellular receptor (JHR), a ligand-activated complex of transcription factors consisting of the JH-binding protein Methoprene-tolerant (MET) and its partner Taiman (TAI). Initial studies indicated significance of post-transcriptional phosphorylation, subunit assembly, and nucleocytoplasmic transport of JHR in JH signaling. However, our knowledge of JHR regulation at the protein level remains rudimentary, partly due to the difficulty of obtaining purified, functional JHR proteins. Here we present a method for high-yield expression and purification of JHR complexes from two insect species, the beetle Tribolium castaneum and the mosquito Aedes aegypti. Recombinant JHR subunits from each species were co-expressed in an insect cell line using a baculovirus system. MET-TAI complexes were purified through affinity chromatography and anion exchange columns to yield proteins capable of binding both the hormonal ligand (JH III) and DNA bearing cognate JH-response elements. We further examined the beetle JHR complex (TcJHR) in greater detail. Biochemical analyses and mass spectrometry confirmed that TcJHR was a 1:1 heterodimer consisting of TcMET and TcTAI proteins, stabilized by the JHR agonist ligand methoprene. Phosphoproteomics uncovered multiple phosphorylation sites in the TcMET protein, some of which were induced by methoprene treatment. Finally, we report a functional bipartite nuclear localization signal, straddled by phosphorylated residues, within the disordered C-terminal region of TcMET. Our present characterization of the recombinant JHR is an initial step towards understanding JHR structure and function.