Recombinant YTHDF2 protein

N6-methylated adenine (m6A) is prevalently present in nearly all RNA types and can be found in all organisms from bacteria to humans. It preferentially appears around stop codons and within long internal exons in mammalian messager RNAs. m6A plays an important role in the efficiency of mRNA splicing, processing, translation efficiency, editing and mRNA stability. m6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs). In mammalian cells, METTL3 (methyltransferase-like 3, also known as IME4, M6A, MT-A70) and METTL14 (methyltransferase-like 14) are two m6A methyltransferases reported to date, which both contain methyltransferase domains. These two proteins form a stable heterodimer core complex of METTL3-METTL14 that functions in cellular m6A deposition on mammalian nuclear RNAs. METTL3 is the catalytically active subunit, while METTL14 plays a structural role critical for substrate recognition.