epitope mapping at the N-terminus of DAD1 of human origin
recommended for detection of DAD1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
DAD1 Background Information Membrane proteins of the endoplasmic reticulum (ER) may be localized by mechanisms that involve retention, retrieval, or a combination of both (1,2). ER localization information has been found in cytoplasmic, transmembrane, or luminal domains (2). Specific retrieval mechanisms have been identified for luminal ER proteins, which contain a KDEL domain, and for type I transmembrane proteins carrying a dilysine motif (2). The mammalian oligosaccharyltransferase (OST) is a protein complex that is composed of four rough ER-specific, type I transmembrane proteins: ribophorins I and II (RI and RII), OST48, and DAD1 (also designated defender against apoptotic death) (1,3,4). The ribophorins are integral membrane glycoproteins that localize exclusively to the rough endoplasmic reticulum (5,6). There is affinity between the cytoplasmically located N-terminal region of DAD1 and the short cytoplasmic tail of OST48 to place DAD1 firmly into the OST complex (3-5). The OST affects the cotranslational N-glycosylation of newly synthesized polypeptides (1).
DAD1 (N-20) 논문정보
DAD1 (N-20): sc-12173 antibody 및 DAD1 (N-20) antibody conjugates를 사용한 논문들을 보세요.
