DDR2 (human, recombinant)

Discoidin domain-containing receptor 2 (DDR2), also known as CD167b, is a receptor tyrosine kinase (RTK) with roles in microenvironmental sensing and the physiological and pathological processes regulated by collagen remodeling. It is composed of an extracellular discoidin domain, discoidin-like domain, and juxtamembrane domain, a transmembrane domain, and an intracellular juxtamembrane domain and kinase domain. DDR2 is expressed in mesenchymal cells, including fibroblasts, myofibroblasts, smooth muscle cells, and chondrocytes, as well as in circulating human neutrophils, and localizes to the cell membrane. Unlike most RTKs that bind soluble ligands, DDR binds to collagen monomers, including type I, II, III, and V fibrillar collagen and non-fibrillar type X collagen. Collagen binding induces autophosphorylation of the intracellular juxtamembrane and kinase domains and recruitment of various proteins to facilitate signal transduction. DDR2 is associated with cartilage and bone damage in patients with rheumatoid arthritis. DDR2 is overexpressed in various cancers, including non-small cell lung cancer (NSCLC), Hodgkin lymphoma, prostate cancer, thyroid carcinoma, and nasopharyngeal carcinomas. Cayman's DDR2 (human, recombinant) protein consists of 389 amino acids, has a calculated molecular weight of 44. kDa, and a predicted N-terminus of Lys22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is ~60 kDa due to glycosylation.