DDR1 (C-20) Antibody: sc-532

DDR1 Background Information
The majority of the large number of receptor tyrosine kinases that have been identified can be categorized into distinct families based on the structure of their extracellular domains. Only a limited number of ligands for the receptors have been described, and while the majority of the ligands identified are soluble factors, an increasing number of receptors have been shown to bind to cell-surface molecules. Discoidin domain receptor 1 (DDR1), previously identified as Cak, for cell adhesion kinase (and also designated MCK-10, EDDR1, NEP, Ptk-3, RTK6, trk E or NTRK4) and discoidin domain receptor 2 (DDR2) comprise a new family of receptor tyrosine kinases involved in cell-cell interactions. Both DDR1 and DDR2 have been shown to be activated by collagen. Evidence suggests that a docking site for the Shc phosphotyrosine binding domain is phosphorylated in response to activation of DDR1 by collagen, whereas collagen activation of DDR2 results in upregulation of matrix metalloproteinase-1 expression.