PathScan^® DPP4/CD26 Sandwich ELISA Kit #81566

DPP4 (CD26) is a type II transmembrane glycoprotein expressed ubiquitously in most tissues and different cell types (1,2). The protein has a short cytoplasmic domain, a transmembrane domain, a flexible stalk fragment, and an extracellular fragment (2). Both the catalytic peptide hydrolase domain and the beta-propeller ligand binding domain are located in the extracellular fragment (2). DPP4 is a multifunctional protein that exists in both a membrane-bound form as well as an extracellular soluble form. As a peptidase, it removes N-terminal dipeptides sequentially from proteins with a proline or alanine as the penultimate P1 amino acid (3,4). DPP4 has been shown to cleave a wide range of substrates, including GLP-1, BNP, substance P, etc. It is also involved in the regulation of related biological functions (5). In addition to its peptidase activity, DPP4 interacts with multiple important cell surface ligands, such as adenosine deaminase, fibronectin, and IGF2 receptor, to influence processes like T cell activation, cell migration, and proliferation (5). Several DPP4 inhibitors have been developed and their effects have been tested in the field of diabetes, cardiovascular disease, and tumor immunity (2,5,6).