The gene for azurocidin is located on the short arm of chromosome 19 and is in a cluster with the genes for proteinase 3 and elastase. All three proteins are serine protease homologues; azurocidin, however, lacks enzymatic activity. It is an antibiotic protein, with monocyte chemotactic and antibacterial activity. The Azurophil granules, specialized lysosomes of the neutrophil, contain at least 10 proteins implicated in the killing of microorganisms. Azurocidin is a member of the serine protease family that includes Cathepsin G, Neutrophil Elastase (NE), and Proteinase 3 (PR3), however, Azurocidin is not a serine proteinase since the active site serine and histidine residues are replaced. Azurocidin has been identified as a modulator of endothelial permeability and an important multifunctional inflammatory mediator. Neutrophils arriving first at sites of inflammation release Azurocidin which acts in a paracrine fashion on endothelial cells causing the development of intercellular gaps and allowing leukocyte extravasation. Azurocidin thus be regarded as a reasonable therapeutic target for a variety of inflammatory disease conditions.