Mouse/Rat Proprotein Convertase 9/PCSK9 Antibody

PC9 (Proprotein convertase subtilisin type 9; also PCSK9 and NARC-1) is a 70‑74 kDa, secreted glycoprotein member of the proteinase K subfamily of subtilases. PC9 functions as a protease that cleaves proproteins at non-basic residues. It also binds to, and promotes, the degradation of LDLR, VLDLR and ApoER2. The mouse PC9 precursor is 694 amino acid (aa) in length, and contains a signal sequence, a 14 kDa, 121 aa prodomain (aa 35‑155), and a 56‑58 kDa, 539 aa mature region (aa 156‑694). The 58 kDa mature region arises from autocatalysis in the ER, and contains a subtilisin-like catalytic domain (aa 166‑432), a modified P-domain (aa 433‑529) and a C-terminal Cys-rich region (aa 530‑694). The prosegment and mature regions remain noncovalently associated. There is one additional PC9 isoform that shows an alternative start site 13 aa upstream of the standard site coupled to a deletion of aa 18‑20. Over aa 156‑694, mouse PC9 shares 93% and 79% aa identity with rat and human PC9, respectively.