epitope mapping within an internal region of Aminopeptidase P1 of human origin
recommended for detection of Aminopeptidase P1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
Aminopeptidase P1 Background Information Aminopeptidases comprise a family of enzymatic proteins that are widely distributed in both eukaryotes and prokaryotes and function to catalyze the removal of amino acids from the N-termini of proteins. Aminopeptidase P1 is proline-specific; it cleaves the N-terminal amino acid where the second residue is proline. It is a mammalian bradykinin-degrading, metal-dependant enzyme that exists in two forms: a membrane-bound form and a cytosolic form. Aminopeptidase P1 is GPI-linked and the membrane-bound form is expressed in all tissues with highest expression in pancreas. Aminopeptidase P1 has been shown to be a receptor for the breast-homing peptide and may therefore be a potential therapeutic target for the treatment and prevention of breast cancer.
