Membrane proteins constitute around 27% of the human proteome and roughly 60% of all therapeutic drugs target membrane proteins, highlighting the importance of this class of proteins. One subfamily o fmembrane proteins is the water channel proteins also known as aqua-porins (AQPs). These membrane-spanning pore proteins are found in all living organisms and selectively facilitate the flux of water across membranes. Thus, AQPs are mainly responsible for maintaining water homeostasis. Some AQPs, however, do possess the ability to mediate transport of other molecules, such as glycerol. In addition, the structural characterization of aquaglyceroporins (AQGPs) is very limited. Therefore, functional and structural characterization of these proteins might reveal previously unknown mechanisms of how fat is stored and released in adipocytes. Due to the ability to selectively facilitate the transport of water molecules, AQPs have also shown to be of great biotechnological interest. Aquaporin A/S was founded in 2005 and by exploiting the exquisite architecture developed by billions of years of evolution, Aquaporin A/S is now able to filter water the way nature does it. However, the production of water filters is limited due to the low abundance of AQPs, and a membrane protein production facility is necessary for upscaling the production. This study is divided into two main focuses; production of human AQPs for biophysical characterization and, identification and largescale production of novel putative AQPs. First, a yeast-based expression system suitable for producing prime quality human membrane proteins is presented. This led to the structural and functional characterization of a human AQGP, namely the hAQP10 found in adipocytes. In vivo and in vitro functional data indicated a gating mechanism upon pH decrease, while structural data and molecular dynamics supported this hypothesis. As a consequence, a gating mechanism in hAQP10 under lipolytic conditions was suggested. Second, a membrane protein production facility was established. Thereby, supporting the manufacturing of water filters at Aquaporin A/S by producing membrane proteins to an annual amount of kilograms. Compared to standard purification of membrane proteins, steps not suitable for up-scaling was avoided. Nine putative AQPs from extremophiles for later implementation into the Aquaporin Inside® Technology was identified and expressed in Saccharomyces cerevisiae. In conclusion, this work provides a thorough study of production and biophysical studies of human AQPs and identification and expression of novel AQPs for industrial use.