DDR1b Extracellular Domain (human, recombinant)

Discoidin domain-containing receptor 1 (DDR1), also known as CD167, is a receptor tyrosine kinase (RTK) with roles in cell migration, proliferation, and differentiation and other physiological and pathological processes regulated by collagen remodeling. It is composed of an extracellular discoidin domain, a transmembrane domain, and intracellular juxtamembrane and kinase domains. DDR1 is selectively expressed in epithelial cells and localizes to the cell membrane. DDR1 undergoes alternative splicing to produce five isoforms, of which three, DDR1a, DDR1b, and DDR1c, are kinase active and two, DDR1d and DDR1e, are kinase domain-deficient. Unlike most RTKs that bind soluble ligands, DDR1 binds to and is activated by fibrillar and non-fibrillar collagens. DDR1b binds directly to talin and enhances integrin beta1-mediated cell migration. Cayman's DDR1b Extracellular Domain (human, recombinant) protein consists of 409 amino acids, has a calculated molecular weight of 45. kDa, and a predicted N-terminus of Asp19 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 55-60 kDa due to glycosylation.