Human RENT1/UPF1 Antibody

UPF1 (Up-frameshift mutation-1; also RENT1, SMG-2 and NORF1) is a 125-130 kDa member of the DNA2/NAM7 helicase family of molecules. It is ubiquitously expressed, and promotes the turnover of mRNA containing premature stop codons. UPF1 is a cytoplasmic factor that contributes to the formation of a UPF complex. During the translation of properly transcribed mRNA, unphosphorylated UPF1 is blocked from interacting with eRF3, a translation initiation factor. In the presence of an improper stop codon, a detection complex termed EJC initiates phosphorylation of UPF1, allowing it to bind to eRF3 and repress translation. Human UPF1 is 1129 amino acids (aa) in length. It contains one C2H2-type Zn finger motif (aa 131-159), an NTPase domain (aa 486-545) and three phosphorylation sites at Ser1107/1127/1129. There are two potential isoforms that show deletions of aa 54-58 and 353-363, respectively. Over aa 351-600, human UPF1 shares 99% aa identity with mouse UPF1.