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The protein encoded by DCP2 is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). Additionally we are shipping DCP2 Antibodies (61) and many more products for this protein.
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results suggest miR-141-3p/200a-3p may be involved in post-transcriptional repression of Dcp2 expression during renal development
ERK-phosphorylated Dcp1a enhances its interaction with the decapping enzyme Dcp2 during early differentiation of 3T3-L1 cells.
Recruitment of DCP1A and DCP2 increases the mRNA degradation capacity of the maturing oocyte so that by the 2-cell stage, most of the maternal mRNA is degraded.
The results showed that DCP1A and DCP2 are critical in the transition from mRNA stability to instability during meiotic maturation and that mRNA degradation must be successful to execute the oocyte-to-zygote transition.
In this study the increase in Irf-7 mRNA within the background of reduced Dcp2 levels was attributed to a stabilization of the Irf-7 mRNA, suggesting that Dcp2 normally modulates Irf-7 mRNA stability.
Like Dcp2, Nudt16 also regulates the stability of a subset of mRNAs including a member of the motin family of proteins involved in angiogenesis.
Human Dcp2 levels and activity are controlled by a competition between decapping complex assembly and Dcp2 degradation.
The data indicates that DCP2 activation by DCP1 occurs preferentially on the EDC4 scaffold, which may serve to couple DCP2 activation by DCP1 with 5'-to-3' mRNA degradation by XRN1 in human cells.
Data show that Y14 interacts directly with the decapping factor Dcp2 and the 5' cap structure of mRNAs via different but overlapping domains.
PNRC2 acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a and Dcp2.
an mRNA decapping enzyme demonstrated to contain intrinsic decapping activity
These data suggest that a human decapping complex containing decapping enzymes hDcp1a and hDcp2 may be recruited to mRNAs containing premature termination codons by the hUpf proteins.
Human Dcp2 is a catalytically active mRNA decapping enzyme that localizes to the cytoplasm
LSm1-7 proteins colocalize with DCP1,DCP2 and Xrn1 in cytoplasmic foci
hDcp2 can specifically bind to and can regulate the stability of a subset of mRNAs
These data support the novel notion of the association between Ro52 with hDCP2 protein in cytoplasmic p-bodies, playing a role in mRNA metabolism in response to cellular stimulation.
The protein encoded by this gene is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It removes the 7-methyl guanine cap structure from mRNA, prior to its degradation from the 5' end. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.
mRNA-decapping enzyme 2
, DCP2 decapping enzyme homolog
, m7GpppN-mRNA hydrolase
, nudix (nucleoside diphosphate linked moiety X)-type motif 20