PC2 (D1E1S) XP^® Rabbit mAb #14013

The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).
Unlike what is observed with furin whose gene invalidation is lethal, inactivation of mouse PC2 by the introduction of a neomycin resistance gene into the third exon of the PCSK2 gene does not alter mouse viability (4). PC2 inactivation leads to alteration of the pancreatic islet cells, in agreement with the involvment of PC2 in the conversion of pro-insulin and pro-glucagon (5). PC2 is also responsible for the processing of several neuroendocrine peptide precursors such as pro-CCK, POMC, and neurotensin (6).