Copper is a vital micronutrient required for the proper metabolic functioning of most prokaryotic and eukaryotic organisms. It plays a pivotal role in the physiology of aerobic organisms, participating in processes such as electron transport, iron metabolism, and the functioning of antioxidant enzymes. However, copper’s reactivity can lead to the generation of free radicals, making its regulation within cells critical to avoid toxicity .
The cutC protein is a cytoplasmic and nuclear protein that can bind one Cu1+ ion per subunit. It is involved in the efflux trafficking of cuprous ions, helping to maintain the balance of copper within cells. The human cutC protein shares significant sequence identity with its counterparts in other species, including 89% with the mouse and 44% with the E. coli CutC proteins .
Recombinant human cutC protein is typically expressed in E. coli and purified using conventional chromatography techniques. The recombinant protein often includes an N-terminal His-tag to facilitate purification. The protein is usually lyophilized from a sterile PBS solution containing glycerol and other protectants to ensure stability during storage .
The cutC protein is primarily used for research purposes, particularly in studies related to copper metabolism and homeostasis. Understanding the function and regulation of cutC can provide insights into various diseases and conditions associated with copper imbalance, such as Wilson’s disease and Menkes disease .