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.，官网链接：https://www.sigmaaldrich.cn/product/mm/mabs1910 默克 科研、开发、生产。 作为生命科学行业的全球领先供应商，我们致力于为科研、生物技术开发和生产，以及制药药物疗法开发和生产提供各类解决方案和服务。

非质量问题不退不换