Disintegrin and metalloproteinase domain-containing protein 10, also known as ADAM10, is a membrane-anchored protease that belongs to the ADAM protease family. ADAMs are type I transmembrane proteins with a large extracellular domain and a shorter cytosolic part, they contain a metalloprotease domain, a disintegrin domain, a cystein-rich domain, an EGF-like domain, a transmembrane domain and a cytoplasmic tail². 37 murine and 22 human ADAMs are known and only some of them contain the catalytically relevant domain (HEXGHXXGXXHD) and are therefore able to cleave the extracellular domains of several membrane-bound proteins in a process known as 'ectodomain shedding'¹.  This process represents a unique and irreversible posttranslational event regulating the function and half-life of many intracellular and extracellular proteins and hence the ADAM family protein's activity is essential for regulation of various cellular functions². ADAM10 has many substrates, among which are cellular adhesion molecules such as cadherin, receptors and ligands³. it is also capable of anti-amyloidogenic proteolysis of the amyloid precursor protein, this is why ADAM10 mutations were shown to be correlated with Alzheimer's disease². In addition, it was shown to involved in various human diseases and disorders such as Huntington's disease, psoriasis, lupus, and multiple types of cancer. The central role of ADAM10 in various cell processes and diseases reveals the potency of ADAM10-targeting drug development as a future therapeutic option².