The Ang II convertase and SARS-COV-2 co-receptor ACE2 is highly expressed on proximal tubules within the kidney. ACE2 is also present in urine and reportedly correlates with various renal pathologies that may reflect enhanced shedding of the peptidase through activation of ADAMs. Indeed, 95 kDa ACE2 is typically detected in urine consistent with a shorter, soluble form of the peptidase; however, the full-length, membrane-bound form of ACE2 (120 kDa) is also evident in urine which is difficult to reconcile with ACE2 shedding. To account for these isoforms, we evaluated ACE2 expression in exosomes isolated from human urine. Morning collections from males [50 to 64 years of age, non-smokers] were immediately processed for exosome isolation by cibacron blue binding of albumin followed by 0.2 μmicron filtration to remove microvesicles and apoptotic bodies, Amicon 100 kDa concentration, and ultracentrifugation (UC) to pellet exosomes. Analysis of the UC pellet fraction revealed the exosomal markers ALIX, CD63 and HSP70, as well as the proximal tubule peptidases neprilysin (NEP) and ACE2. Exosomal ACE2 content was 45 ± 11 ng/mL (mean ± SEM; N=5) by ELISA and exosomal activity hydrolyzed Ang II to Ang-(1-7) that was abolished by the ACE2 inhibitor MLN4760. Fluorescent nanotracking analysis (f-NTA) with Alexa Fluor antibodies and CellMask Deep Red membrane stain (CMDR) demonstrate a similar density of ACE2+ and NEP+ exosomes that were ~50% of total urinary exosomes (*P<0.05 vs. CD63+, N=3) while particle sizes were comparable and in the expected range of exosomes (100-150 nm). We conclude that human urinary exosomes express functional ACE2 which may originate from proximal tubule release.