Mouse/Rat DARC PE-conjugated Antibody

DARC (Duffy Antigen Receptor for Chemokines; also CD234) is a 40-46 kDa glycoprotein member of the Duffy family of silent heptahelical chemokine receptors. It is expressed in liver and on select neurons, erythrocytes and the endothelium of postcapillary venules. Unlike traditional chemokine receptors, DARC cannot signal through G-proteins as it lacks a DRYLAIVHA cytoplasmic motif. DARC has three potential functions: first, it binds circulating inflammatory-type chemokines, serving as a repository for future chemokine release; second, it acts as a vehicle by which chemokines are transported from the abluminal to the luminal side of endothelium; and third, it complexes with signal-transducing chemokine receptors to create a nonsignaling heterodimer. Mouse DARC is 334 amino acids (aa) in length. It contains a 62 aa N-terminal extracellular region, and a 28 aa C-terminal cytoplasmic tail. There is one potential splice variant that shows a 42 aa substitution for aa 133-334. Collectively, over the four extracellular domains (aa 1-62, 115-127, 186-205, 264-285), mouse DARC shares 52% and 75% aa identity with human and rat DARC, respectively.