Recombinant Human ADIPOR2 protein is produced using an in vitro cell-free expression system derived from *E. coli*. This system employs whole-cell extracts that contain the necessary components for protein synthesis, including transcription, translation, and post-translational modification. By supplementing the cell-free extract with cofactors, the full-length ADIPOR2 protein can be synthesized within a few hours. While this method offers advantages such as protein synthesis without cell culturing and the ability to co-express multiple proteins, it is not suitable for large-scale production.
ADIPOR2 is primarily expressed in the liver. It acts as a receptor for adiponectin, a hormone secreted by adipocytes, and plays a crucial role in regulating glucose and lipid metabolism. Upon binding adiponectin, ADIPOR2 activates PPARα, a nuclear receptor, leading to increased fatty acid catabolism. This process involves upregulating genes responsible for fatty acid transport, binding, activation, and fatty acid β-oxidation in peroxisomes and mitochondria. Conversely, ADIPOR2 deficiency reduces PPARα activity. The sensitivity and resistance to adiponectin mediated by ADIPOR2 in hepatocytes have been shown to modulate steatohepatitis progression by altering PPARα activity and reactive oxygen species (ROS) accumulation.