This recombinant Human NOX1 protein is a full-length protein expressed in vitro using a cell-free E. coli system. Its purity is greater than or equal to 85%, as determined by SDS-PAGE. Cell-free protein expression involves the in vitro synthesis of a protein using translation-compatible extracts from whole cells. Essentially, these extracts contain all the necessary macromolecules and components required for transcription, translation, and even post-translational modification. These components include RNA polymerase, regulatory protein factors, transcription factors, ribosomes, and tRNA. When supplemented with cofactors, nucleotides, and the specific gene template, these extracts can synthesize proteins of interest within a few hours.
NOX1 is predominantly expressed in colon epithelium and plays a crucial role in maintaining the epithelial barrier and mucosal homeostasis. It also promotes wound healing in the intestinal mucosa by activating focal cell-matrix adhesion proteins and cell motility. NOX1 primarily exerts its functions during tissue damage and repair by modulating the activity of repair cells, including epithelial cells, fibroblast cells, endothelial cells, and smooth muscle cells. NOX1 contributes to the rapid generation of reactive oxygen species (ROS) in response to IL-13 and interferon-gamma stimulation in human intestinal epithelial cells. NOX1 and its generated ROS further participate in intracellular signaling processes regulating the expression of genes involved in cell proliferation, differentiation, and tissue repair.