||Originally detected as a gene upregulated during apoptosis in rat neuronal cells, bwd has been characterized with high enrichment within restricted areas of the brain and for encoding a protein that is a member of the WD-repeat protein family. Members of this protein family are defined by a structural motif, the beta-propeller, that enables them to complex and regulate a wide functional array of cellular proteins. A functional binding partner for BWD has yet to be evinced; however, a recent yeast two-hybridization yielded evidence that STAT3, a ubiquitously expressed signal transducer/gene regulator involved in the regulation of a vast assortment of cellular processes, may complex with BWD. In binding with STAT3, BWD could potentially regulate, at a cytoplasmic or transcriptional level, numerous essential cellular processes. To discover and characterize this interaction, various co-immunoprecipitation experiments were carried out on protein extracts of 3T3 mouse fibroblast cells to isolate the BWD-STAT3 complex. These experiments were done both with and without cytokine activation of STAT3, as well as with overexpression of both proteins using epitope-tagged expression vectors in the cells. The subsequent Western blot immunodetection found no evidence of BWD and STAT3 in complex in any of the above conditions, denoting the prospect that this interaction is either not real or, like many protein-protein interactions, very type-specific (cell-type, signal-type, etc.) and is simply not present in the conditions study here.