anti-LRRFIP1 Antibody from antibodies-online

Supplier Page

Supplier Page from
antibodies-online for
anti-LRRFIP1 Antibody

Description

Product Characteristics:
LRRFIP1 is an 738 amino acid human protein whose rodent counterpart is known as Lrrfip1 (also designated FLAP in mouse). LRRFIP1 is also believed to control smooth muscle cell proliferation following arterial injury through PDGF-A repression. The N-terminus of LRRFIP1 shows high homology to the coiled-coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I, and the interaction of LRRFIP1 with the LRR of Flightless I has been confirmed. LRRFIP1 does not bind single-stranded DNA or RNA significantly and binds double-stranded DNA weakly. In contrast, LRRFIP1 binds double-stranded RNA with high affinity, and two molecules of LRRFIP1 bind the TaR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. Flightless I has a C-terminal TaR-like domain which binds Actin and therefore the association of LRRFIP1 with the LRR of Flightless I may provide a link between the Actin cytoskeleton and RNA in mammalian cells.

Subcellular location: Cytoplasm, Nucleus

Synonyms: FLAP 1, FLAP1, FLIIAP 1, FLIIAP1, GC binding factor 2, GC-binding factor 2, GCF 2, GCF2, HUFI 1, HUFI1, Leucine rich repeat in FLII interacting protein 1, Leucine rich repeat flightless interacting protein 1, Leucine-rich repeat flightless-interacting protein 1, LRR FLII interacting protein 1, LRR FLII-interacting protein 1, LRRF1_HUMAN, LRRFIP 1, Lrrfip1, MGC10947, MGC119738, MGC119739, NEDD8 conjugating enzyme, TAR RNA interacting protein, TAR RNA-interacting protein, Transcription factor 9 like, TRIP.

Target Information: Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding