The enzyme gamma-glutamyltransferase (GGT) has a substantial role in the metabolism of glutathione (γ-glutamyl-cysteinyl-glycine; GSH). For maintaining adequate levels of intracellular GSH, GGT catalyses the degradation of extracellular GSH, thus providing component amino acids that are then available for further intracellular GSH production. Within the cell GSH functions as a major antioxidant, neutralising reactive oxygen compounds and free radicals. The enzyme encoded by human gamma-glutamyltranspeptidase-1 (GGT1; CD224) gene catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. The enzyme is composed of a heavy chain and a light chain, which are derived from a single precursor protein, and is present in tissues involved in absorption and secretion. GGT expression is found predominantly on the luminal surface of secretory epithelial cells, especially of the hepato-biliary tract, the pancreas and the kidneys. Abnormal GGT expression is found in several human tumours, including breast cancer, ovarian cancer and cervical cancer.

Full-length mature human CD224 cDNA (28-569aa, derived from BC025927) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal and expressed in E.coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used f in vitro human glutathione metabolism mediated apoptosis regulation study with this protein as coating or matrix protein.

2. May be used for protein-protein interaction assay development.

3. Potential biomarker protein for various cancer, such as endometrial cancer,

4. As antigen for specific antibody production.