PRCP (prolylcarboxypeptidase) is a lysosomal serine carboxypeptidase that cleaves C-terminal proline residues from peptides, regulating bioactive molecules like angiotensin II, angiotensin III, and des-Arg⁹-bradykinin. Initially identified in the 1970s, PRCP is involved in the renin-angiotensin system (RAS), blood pressure modulation, and inflammatory pathways. It plays dual roles in homeostasis and disease: while its enzymatic activity helps maintain vascular tone and fluid balance, dysregulation is linked to hypertension, obesity, diabetes, and cancer progression. PRCP also activates prekallikrein in the kinin system, connecting it to coagulation and inflammation. Antibodies against PRCP are vital tools for detecting its expression in tissues (e.g., endothelial cells, kidneys, placenta) and studying its cellular localization via techniques like immunohistochemistry or Western blot. Recent research explores PRCP's therapeutic potential, including inhibitors for metabolic disorders and biomarkers for cardiovascular diseases. However, its precise mechanisms in pathologies like tumor angiogenesis remain under investigation. PRCP antibodies thus serve as critical reagents for unraveling its physiological roles and translational applications.