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Decapping is a key step in general and regulated mRNA decay. Additionally we are shipping DCP1A Proteins (5) and many more products for this protein.
Showing 10 out of 85 products:
Human Monoclonal DCP1A Primary Antibody for IF, ELISA - ABIN565925
Aizer, Brody, Ler, Sonenberg, Singer, Shav-Tal: The dynamics of mammalian P body transport, assembly, and disassembly in vivo. in Molecular biology of the cell 2008
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Human Monoclonal DCP1A Primary Antibody for WB - ABIN395639
Swetloff, Conne, Huarte, Pitetti, Nef, Vassalli: Dcp1-bodies in mouse oocytes. in Molecular biology of the cell 2009
Show all 5 references for 395639
Human Monoclonal DCP1A Primary Antibody for IF, WB - ABIN396083
Sowa, Bennett, Gygi, Harper: Defining the human deubiquitinating enzyme interaction landscape. in Cell 2009
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Cow (Bovine) Polyclonal DCP1A Primary Antibody for WB - ABIN2781065
Lehner, Sanderson: A protein interaction framework for human mRNA degradation. in Genome research 2004
Human Polyclonal DCP1A Primary Antibody for ELISA, WB - ABIN185579
Cougot, Babajko, Séraphin: Cytoplasmic foci are sites of mRNA decay in human cells. in The Journal of cell biology 2004
PKR (show EIF2AK2 Antibodies)-induced translational inhibition appears to be specific to Dcp1a because the expression of other P-body components, Pan2 (show PAN2 Antibodies), Pan3 (show PCSK1N Antibodies), Ccr4 (show CCR4 Antibodies), or Caf1 (show CNOT7 Antibodies), did not result in the inhibition of poliovirus gene expression or induce eIF2alpha (show EIF2A Antibodies) phosphorylation.
ERK (show EPHB2 Antibodies)-phosphorylated Dcp1a enhances its interaction with the decapping enzyme Dcp2 (show DCP2 Antibodies) during early differentiation of 3T3-L1 cells.
Recruitment of DCP1A and DCP2 (show DCP2 Antibodies) 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 (show DCP2 Antibodies) 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.
Data show the presence of P-body-like foci in mouse oocytes, as revealed by the presence of Dcp1a and the colocalization of RNA-associated protein 55 (RAP55 (show LSM14A Antibodies)) and the DEAD box RNA helicase (show DDX56 Antibodies) Rck/p54 (show DDX6 Antibodies).
Overexpression of wild-type SMIF enhanced expression of TGFbeta/BMP (show TGFb Antibodies) regulated genes, whereas a dominant-negative SMIF mutant suppressed expression.
These findings suggest a novel post-translational modification that may influence the function of Dcp1a in response to various physiological cues.
The E3 ligase TRAF6 (show TRAF6 Antibodies) binds to DCP1a and indirectly regulates DCP1a phosphorylation, expression of decapping factors, and gene-specific mRNA decay.
DCP1A rs11551405 may have a prognostic effect on survival of CM patients.
The assembly of EDC4 (show EDC4 Antibodies) and Dcp1a into processing bodies is critical for the translational regulation of IL-6 (show IL6 Antibodies).
Phosphorylation at serine 315, serine 319, and threonine 321 of DCP1A modulates IL-8 (show IL8 Antibodies) expression during respiratory syncytial virus infection.
The data indicates that DCP2 (show DCP2 Antibodies) activation by DCP1 (show ACE Antibodies) occurs preferentially on the EDC4 (show EDC4 Antibodies) scaffold, which may serve to couple DCP2 (show DCP2 Antibodies) activation by DCP1 (show ACE Antibodies) with 5'-to-3' mRNA degradation by XRN1 (show XRN1 Antibodies) in human cells.
Malin (show NHLRC1 Antibodies) regulates the recruitment of mRNA-decapping enzyme 1A (Dcp1a) to processing bodies.
PNRC2 (show PNRC2 Antibodies) acts in synergy with Dcp1a to stimulate the decapping activity of Dcp2 (show DCP2 Antibodies) by bridging the interaction between Dcp1a and Dcp2 (show DCP2 Antibodies).
Reveal DCP1a as a multifunctional regulator of mRNA expression and suggest a role for JNK (show MAPK8 Antibodies) kinase phosphorylation in controlling the subcellular localization of DCP1a in response to stress or inflammatory stimuli.
Data show the presence of P-body-like foci in mouse oocytes, as revealed by the presence of Dcp1a and the colocalization of RNA-associated protein 55 (RAP55 (show LSM14A Antibodies)) and the DEAD box RNA helicase (show DDX5 Antibodies) Rck/p54 (show DDX6 Antibodies).
Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts with the nonsense-mediated decay factor hUpf1 and may be recruited to mRNAs containing premature termination codons. This protein also participates in the TGF-beta signaling pathway.
DCP1 decapping enzyme homolog A (S. cerevisiae)
, DCP1 decapping enzyme homolog A
, mRNA-decapping enzyme 1A
, MAD homolog 4 interacting transcription coactivator 1
, MAD homolog 4-interacting transcription coactivator 1
, Smad4-interacting transcriptional co-activator
, decapping enzyme
, transcription factor SMIF
, decapping enzyme hDcp1a
, putative protein product of Nbla00360