Dipeptidyl-peptidase 2 is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.predicted 492-amino acid protein has a calculated molecular mass of 54.3 kD and contains the consensus sequence for the active-site serine residue of serine-type proteases. It shares 42% amino acid identity with the carboxypeptidase PRCP, with higher identity at the putative active-site residues. Northern blot analysis detected a 1.7-kb transcript in PBMCs and Jurkat T cells. SDS-PAGE analysis showed expression of a 58-kD protein.