Anti-Signal peptide peptidase-like 3 Antibody, clone 7F9 clone 7F9, from mouse

Signal peptide peptidase-like 3 (UniProt: Q8TCT6; also known as SPP-like 3, Intramembrane protease 2, IMP-2, Presenilin homologous protein 1, PSH1, Presenilin-like protein 4, SPPL3) is encoded by the SPPL3 (also known as IMP2) gene (Gene ID: 121665) in human. SPPL3 is a multi-pass transmembrane protein that is shown to be widely expressed and is highly conserved in multicellular eukaryotes. Three isoforms of SPPL3 have been described that are produced by alternative splicing. It is a member of the intramembrane-cleaving GxGD proteases. It acts as an intramembrane protease that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. It can also act as a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifying glycosidases and glycosyltransferases. It is also shown to catalyze the intramembrane cleavage of the envelope glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy virus independent of prior ectodomain shedding by furin or furin-like proprotein convertase-mediated cleavage proteolysis. The first transmembrane domain of SPPL3 may act as a type I signal anchor. SPPL3 also contains a PAL motif (aa 342-344) that is required for normal active site conformation.