Anti-TRIR antibodies are used in the immunodetection of the protein telomerase RNA component interacting RNase. In humans, the canonical protein has a reported length of 176 amino acid residues and a mass of 18.4 kDa. It is notably widely expressed in many tissue types. TRIR is a reported exoribonuclease that is part of the telomerase RNA 3' end processing complex and which has the ability to all four unpaired RNA nucleotides from 5' end or 3' end with higher efficiency for purine bases. Synonyms for this target antigen include exoribonuclease TRIR, uncharacterized protein C19orf43, and My029 protein. TRIR gene orthologs have been reported in the mouse, rat, bovine, frog, zebrafish and chimpanzee species. ELISA, Western Blot, Immunocytochemistry, Immunofluorescence, and Immunohistochemistry are common applications for TRIR antibodies.