CXCR2/IL-8 RB-Fluorescein Labeled

The human C-X-C chemokine IL-8 is a potent neutrophil chemotactic and activating factor (1). Two distinct cell surface receptors can interact with the IL-8 molecule. These two structures are known as IL-8RA (type I or CXCR-1) and IL-8 RB (type II or CXCR-2) (2, 3). The two receptors share 77% amino acid homology and are both members of the rhodopsin superfamily of G protein-linked receptors that span the cell membrane with seven hydrophobic transmembrane domains. Of the two IL-8 receptors, only IL-8RA exclusively binds IL-8 (4). A third IL-8 binding structure, known as the Duffy blood group antigen, has been identified on red blood cells (5). IL-8RA expression has been documented on neutrophils, monocytes and a small population of T cells (2). The CXCR-2 receptor has the ability to bind a variety of chemokines, including IL-8, GROα, β and γ, NAP-2 and ENA-78. 

Images: A. Typical staining observed with FAB331F on mouse cells transfected with the human CXCR-1, CXCR-2 or CXCR-4 gene. An isotype control staining of the CXCR-2 transfected cells is also shown. B. Typical staining observed with FAB331F on human peripheral granulocytes. An isotype-matched control staining of the same granulocytes is also shown.