epitope mapping near the C-terminus of Thyroid receptor interacting protein 15 of human origin
recommended for detection of TRIP15 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
TRIP15 Background Information TRIP1-TRIP15 genes encode thyroid hormone receptor ∫ (TR ∫)-binding proteins. TRIP15, along with Cops2 and Alien comprise the second subunit (CSN2) of the COP9 signalosome (CSN), an eight-subunit complex with a variety of functions. CSN regulates Skp1-cullin-F-box protein (SCF) ubiquiting ligases by deconjugating Nedd8 from the Cul1 component of the SCF, and also associates with protein kinase activities targetting p53, c-Jun, and IkappaB. Consequently, inhibition of SCF ubiquitin ligase activity occurs, and cell cycle progression halts at the transition from G1 to S phase. TRIP15 contains an acidic region in the N terminus, a putative zinc finger in the C terminus, and a central hydrophobic core region flanked by 2 putative alpha-helical structures and a nuclear localization signal.
