AZGP1

Alpha-2-Glycoprotein 1 Zinc-Binding, also known as Zinc-alpha-2-glycoprotein (ZAG), is a glycoprotein encoded by the AZGP1 gene. It was first isolated from human plasma in 1961 and named for its distinctive electrophoretic mobility within the alpha-2 region and its ability to bind zinc . This protein has a molecular weight of approximately 38-40 kDa .

ZAG is structurally similar to major histocompatibility complex (MHC) class I molecules . It is a soluble protein that stimulates lipolysis, the breakdown of lipids, and plays a role in the regulation of body weight . ZAG is secreted by various tissues and is found in body fluids such as plasma, urine, and seminal fluid .

Despite its presumed immunological function, the role of ZAG in tumor immunity is not fully understood. Recent studies have suggested that ZAG may act as an immunoregulatory factor in the tumor microenvironment . For instance, in breast cancer tissues, ZAG expression has been associated with decreased infiltration of immune cells such as monocytes, macrophages, and myeloid-derived suppressor cells . This suggests that ZAG may influence the immune response in cancer by modulating the phenotype of macrophages .

Recombinant human Alpha-2-Glycoprotein 1 Zinc-Binding (AZGP1) is produced using E. coli expression systems . The recombinant form retains the biological activity of the native protein, including its ability to bind zinc and stimulate lipolysis . It is commonly used in research applications such as enzyme-linked immunosorbent assays (ELISA), Western blotting (WB), and immunoprecipitation (IP) .

ZAG has been implicated in various diseases, including cancer and metabolic disorders . Its role in stimulating lipolysis makes it a potential target for obesity and related metabolic conditions . Additionally, its immunoregulatory properties suggest that it could be a valuable biomarker or therapeutic target in cancer .