epitope mapping near the C-terminus of puromycin-sensitive aminopeptidase of human origin
recommended for detection of puromycin-sensitive aminopeptidase of mouse, rat and human origin by ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
PSAP Background Information Puromycin-sensitive aminopeptidase (PSA or PSAP) is a 100kDa zinc metallopeptidase which degrades neuropeptides by removing amino acid residues from the amino-terminus. The protein is the most abundant aminopeptidase in the brain, however it is not exclusive to that organ. It is localized primarily in the cytoplasm, and plays a role in the metabolism of neuropeptides in nerve terminals and synaptic clefts. The human PSA gene maps to chromosome 17q 2-32.