GS/Fut8 Knockout Cell Line-CHO-K1

Glutamine synthetase (GS), also known as glutamine ammonia ligase, is a key enzyme in amino acid metabolism. It catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine, one of the 20 standard amino acids used in protein synthesis. This reaction not only produces glutamine, an important metabolite involved in various physiological processes, but also plays an important role in the detoxification of ammonia, a potential byproduct of cellular metabolism. Many studies have linked GS dysregulation to pathological conditions, highlighting the importance of this enzyme. In hepatic encephalopathy, decreased GS activity is associated with elevated blood ammonia levels, leading to neurological dysfunction. In cancer, GS is often upregulated in tumor cells, providing them with the necessary glutamine to promote anabolic growth and proliferation. Fucosyltransferase 8 (FUT8) is an enzyme encoded by the FUT8 gene and is a member of the glycosyltransferase family. It catalyzes the transfer of fucose, a hexose, from GDP-fucose to the innermost N-acetylglucosamine (GlcNAc) residue of N-glycans to form core fucosylation. This specific modification plays a key role in the structural and functional diversity of glycoproteins. FUT8 is essential in various biological processes, such as cell signaling, cell adhesion, and immune responses. The activity and expression levels of this enzyme are tightly regulated, and any alterations can have profound physiological consequences. FUT8 dysregulation has been implicated in a variety of pathological conditions, including cancer, inflammation, and innate diseases. In cancer, aberrant core fucosylation is often associated with tumor progression and metastasis.