Anti-RIP140 Antibody, clone 6D7 clone 6D7, from mouse

Nuclear receptor-interacting protein 1 (UniProt: P48552; also known as Nuclear factor RIP140, Receptor-interacting protein 140) is encoded by the NRIP1 gene (Gene ID: 8204) in human. RIP140 is a nuclear protein that is localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1. It is expressed in liver in a circadian manner. RIP140 contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors. The C-terminal LTKTNPILYYMLQK motif is required for ligand-dependent interaction with retinoic acid (RA) receptor-alpha (RARA) and retinoid X receptor beta (RXRB) homodimers and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB. It also contains at least four autonomous repression domains (RD1-4). RD1 functions via a histone deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4 can function by HDAC-dependent or independent mechanisms, depending on cell type. RIP140 Acetylation regulates its nuclear translocation and co-repressive activity of RIP140 is regulated by its acetylation, which is shown to abolish its interaction with C-terminal-binding protein 1 (CTBP1). Several glucocorticoid responses are shown to be deregulated by RIP140 possibly via an interaction between the glucocorticoid receptor (GR), which prevents binding of true co-activator with GR. (Ref.: Subramaniam N, et al. (1999). J. Biol. Chem. 274(25):18121-7).