Anti-RENT1/hUPF1 Antibody Picoband® (monoclonal, 11E7) Fluoro647 Conjugated

Regulator of nonsense transcripts 1 is a protein that in humans is encoded by the UPF1 gene. This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD) . When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. And this protein is located only in the cytoplasm. When translation ends, it interacts with the protein that is a functional homolog of yeast Upf2p to trigger mRNA decapping. Use of multiple polyadenylation sites has been noted for this gene. Alternative splicing results in multiple transcript variants.

ATP dependent helicase RENT1 antibody; ATP-dependent helicase RENT1 antibody; Delta helicase antibody; FLJ43809 antibody; FLJ46894 antibody; HUPF 1 antibody; hUpf1 antibody; KIAA0221 antibody; Nonsense mRNA reducing factor 1 antibody; NORF 1 antibody; NORF1 antibody; pNORF 1 antibody; pNORF1 antibody; Regulator of nonsense transcripts 1 antibody; RENT 1 antibody; RENT1 antibody; RENT1_HUMAN antibody; Smg 2 antibody; Smg 2 homolog nonsense mediated mRNA decay factor antibody; UP Frameshift 1 antibody; Up frameshift mutation 1 homolog (S. cerevisiae) antibody; Up frameshift mutation 1 homolog antibody; Up frameshift suppressor 1 homolog antibody; Up-frameshift suppressor 1 homolog antibody; UPF 1 antibody; UPF 1 regulator of nonsense transcripts homolog antibody; upf1 antibody; UPF1 regulator of nonsense transcripts homolog antibody; Yeast Upf1p homolog antibody

Apoptosis, Cancer, Cardiovascular, G Protein Signaling, Heterotrimeric G Proteins, Neural Signal Transduction, Neurology Process, Neuroscience, Nucleotide Messenger, Second Messenger, Signal Transduction, Signaling Pathway, Small G Proteins

RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD. Essential for embryonic viability.

1. Entrez Gene: UPF1 UPF1 regulator of nonsense transcripts homolog (yeast) . 2. Applequist SE, Selg M, Raman C, Jack HM (March 1997) . Cloning and characterization of HUPF1, a human homolog of the Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein. Nucleic Acids Res 25 (4) : 814–21. 3. Perlick HA, Medghalchi SM, Spencer FA, Kendzior RJ Jr, Dietz HC (November 1996) . Mammalian orthologues of a yeast regulator of nonsense transcript stability. Proc Natl Acad Sci U S A 93 (20) : 10928–32.