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Description
Atypical chemokine receptor 1 (UniProt: Q16570, also known as Duffy antigen/chemokine receptor, DARC, Fy glycoprotein, GpFy, Glycoprotein D, Plasmodium vivax receptor, CD234) is encoded by the ACKR1 (also known as DARC, FY, GPD) gene (Gene ID: 2532) in human. DARC is a multi-pass membrane protein of the G-protein coupled receptor 1 family with four extracellular domains, seven transmembrane domains, and four cytoplasmic domains. Its N-terminal glycosylated extracellular domain carries the Duffy blood group antigens Fya and Fyb. It is present mainly on erythrocytes and endothelial cells of post-capillary venules of various tissues. DARC serves as a promiscuous receptor for a number of pro-inflammatory CC and CXC chemokines but lacks signal transduction ability. However, it controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. It is reported to regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms. When expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes. However, when expressed in erythrocytes, it serves as blood reservoir of cognate chemokines and a chemokine sink, buffering potential surges in plasma chemokine levels. Clone NaM185-2C3 recognizes a linear epitope, the essential portion of which is localized in amino acids 22-26 where all amino acid residues of the epitope, except Asp, are essential for antibody-binding. (Ref.: Grodecka, M., et al. (2010). Acta Biochimica Polonica. 57(1), 49-53, Wasniowska, K., et al. (2002). Transfusion Med. 12(3), 205-211).
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