The ADAMs (A disintegrin and metalloprotease) family of transmembrane proteins belongs to the zinc protease superfamily. These proteins have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, as well as a cytoplasmic domain that specifies binding sites for various signal transducing proteins. The ADAMs family is involved in controlling membrane fusion, cytokine and growth factor shedding, cell migration, muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer also involve ADAMs family members. The ADAMs family consists of 19 *adam* genes in humans, with some members being expressed exclusively or predominantly in the testis and others showing a more broad somatic distribution. Alternative splicing produces multiple isoforms of ADAMs, which can have different subcellular localizations and activities. The prodomain of ADAMs is involved in their maturation and activation, while the metalloprotease domain is responsible for proteolytic activity. The disintegrin domain binds to integrin receptors, and the cysteine-rich and EGF-like domains may play roles in membrane fusion and cell adhesion. The cytoplasmic tails of ADAMs contain motifs that regulate metalloprotease activity, cell signaling, and maturation. ADAMs are involved in the shedding of cytokines and cytokine receptors, growth factors and growth factor receptors, and the processing of other molecules such as insulin-like growth factor-binding proteins and amyloid precursor protein. The regulation and specificity of sheddase activity in ADAMs are complex and involve multiple factors, including protein-protein interactions and post-translational modifications.The ADAMs (A disintegrin and metalloprotease) family of transmembrane proteins belongs to the zinc protease superfamily. These proteins have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, as well as a cytoplasmic domain that specifies binding sites for various signal transducing proteins. The ADAMs family is involved in controlling membrane fusion, cytokine and growth factor shedding, cell migration, muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer also involve ADAMs family members. The ADAMs family consists of 19 *adam* genes in humans, with some members being expressed exclusively or predominantly in the testis and others showing a more broad somatic distribution. Alternative splicing produces multiple isoforms of ADAMs, which can have different subcellular localizations and activities. The prodomain of ADAMs is involved in their maturation and activation, while the metalloprotease domain is responsible for proteolytic activity. The disintegrin domain binds to integrin receptors, and the cysteine-rich and EGF-like domains may play roles in membrane fusion and cell adhesion. The cytoplasmic tails of ADAMs contain motifs that regulate metalloprotease activity, cell signaling, and maturation. ADAMs are involved in the shedding of cytokines and cytokine receptors, growth factors and growth factor receptors, and the processing of other molecules such as insulin-like growth factor-binding proteins and amyloid precursor protein. The regulation and specificity of sheddase activity in ADAMs are complex and involve multiple factors, including protein-protein interactions and post-translational modifications.