Reliable detection of indoleamine 2,3 dioxygenase-1 in murine cells and tissues.

The essential amino acid tryptophan is catabolized by the first and rate-limiting enzyme of the kynurenine pathway, indoleamine 2,3-dioxygenase-1 (IDO1). IDO1 is implicated in several diseases including cancer, chronic infection, autoimmune disorders and neurodegenerative diseases. Antibodies that accurately recognize human IDO1 protein in situ in tissues are available, including clone 10.1 generated in our laboratory and now widely available through commercial sources (Muller, DuHadaway, Sutanto-Ward, Donover, & Prendergast, 2005). However, until recently, there were no antibodies available to accurately detect murine IDO1 protein in situ in preclinical mouse models of disease. Such probes are crucial to establish cellular mechanisms since IDO1 appears to act in different cell types depending on disease context, but reliable probes have been elusive in the field. Recently we addressed this issue with the development of IDO1 monoclonal antibody 4B7, the specificity of which was fully validated by a lack of binding to tissues derived from mice that are genetically deficient in IDO1. This antibody offers a reagent that is unique in the field for specifically recognizing the enzyme in murine tissues, addressing the acute need for a reliable tool to conduct immunohistology in preclinical disease models.