Anti-Dcp2 serum, from rabbit

m7GpppN-mRNA hydrolase (UniProt: Q8IU60; also known as EC:3.6.1.62, Nucleoside diphosphate-linked moiety X motif 20, Nudix motif 20, mRNA-decapping enzyme 2, hDpc) is encoded by the DCP2 (also known as NUDT20) gene (Gene ID: 167227) in human. Dcp2 is a manganese-dependent decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. It removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Dcp2 contains a functional Nudix (nucleotide diphosphate linked to an X moiety) motif (aa 95-226) that is essential for its decapping activity. Two isoforms of Dcp2 have been described that are produced by alternative splicing. Dcp2 is reported to play a role in replication-dependent histone mRNA degradation. It has higher activity towards mRNAs that lack a poly(A) tail and does not display any activity towards a cap structure lacking an RNA moiety. Dcp2 is predominantly cytoplasmic, however, a small amount may also be found in the nucleus. Higher expression of Dcp2 has been reported in subjects with celiac disease with higher levels in the nuclear fraction. (Ref.: Wang, Z., et al. (2002). Proc. Natl. Acad. Sci. USA 99(20); 12663-12668; Castellanos-Rubio, A., et al. (2016). Science 352(6281); 91-95).