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Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. Additionally we are shipping EIF4G2 Proteins (4) and many more products for this protein.
Showing 10 out of 111 products:
Human Monoclonal EIF4G2 Primary Antibody for FACS, WB - ABIN265943
Levy-Strumpf, Deiss, Berissi, Kimchi: DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death. in Molecular and cellular biology 1997
Show all 6 references for ABIN265943
Human Monoclonal EIF4G2 Primary Antibody for WB - ABIN394226
Frank, Virgili, Sonenberg, Nagar: Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5. in Acta crystallographica. Section F, Structural biology and crystallization communications 2010
Show all 5 references for ABIN394226
Human Polyclonal EIF4G2 Primary Antibody for WB - ABIN1944751
Imataka, Olsen, Sonenberg: A new translational regulator with homology to eukaryotic translation initiation factor 4G. in The EMBO journal 1997
Show all 3 references for ABIN1944751
Human Monoclonal EIF4G2 Primary Antibody for IHC (p), ELISA - ABIN560721
Katsogiannou, Andrieu, Baylot, Baudot, Dusetti, Gayet, Finetti, Garrido, Birnbaum, Bertucci, Brun, Rocchi: The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets. in Molecular & cellular proteomics : MCP 2014
Chicken Polyclonal EIF4G2 Primary Antibody for WB - ABIN2778774
Nousch, Reed, Bryson-Richardson, Currie, Preiss: The eIF4G-homolog p97 can activate translation independent of caspase cleavage. in RNA (New York, N.Y.) 2007
The Coxsackievirus B3 protease 2A-mediated cleavage of DAP5 results in the production of two truncates that exert differential effects on protein translation of the IRES-containing genes, leading to enhanced host cell death.
Knockdown of EIF4G2 recapitulated the effects of mir (show MLXIP Antibodies)-139, whereas restoring EIF4G2 expression rescued the mir (show MLXIP Antibodies)-139 phenotype. elevated miR (show MLXIP Antibodies)-139-5p expression is associated with a favorable outcome in acute myeloid leukemia (show BCL11A Antibodies).
findings provide the first mechanistic insights into the function of DAP5 as a selective regulator of cap-independent translation
Our results provide evidence that the tumor suppressor effect of miR (show MLXIP Antibodies)-520c-3p is mediated through repression of translation while inducing senescence and that eIF4GII (show EIF4G3 Antibodies) is a key effector of this anti-tumor activity.
DAP5, a translation initiation factor shown to positively regulate the translation of various internal ribosome entry sites containing mRNAs, promotes internal ribosome entry site-driven translation of p53 (show TP53 Antibodies) mRNA.
DAP5/p97 and DAP5/p86 enhanced the translation of the anti-apoptotic protein Bcl-2 (show BCL2 Antibodies) and inhibited cisplatin-induced apoptosis
Multiple isoforms of eIF4GII (show EIF4G3 Antibodies) arise from multiple promoters & alternative splicing events. A non-canonical CUG initiation codon extends the eIF4GII (show EIF4G3 Antibodies) N-terminus. The eIF4GII (show EIF4G3 Antibodies) N-terminus plays an alternative role in initiation factor assembly.
crystal structure of C-terminal region (residues 540-897) of p97/EIF4G2 (at 2.0 Angstrom resolution): sequence/structure homology with EIF4G1 (show EIF4G1 Antibodies)
crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5 is presented.
The caspase (show CASP3 Antibodies)-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins
analysis of the tandem MA-3 (show PDCD6 Antibodies) region of Pdcd4 (show PDCD4 Antibodies) protein and characterization of its interactions with eIF4A (show EIF4A1 Antibodies) and eIF4G (show EIF4G1 Antibodies)
Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. The protein encoded by this gene shares similarity with the C-terminal region of eIF4G that contains the binding sites for eIF4A and eIF3\; eIF4G, in addition, contains a binding site for eIF4E at the N-terminus. Unlike eIF4G, which supports cap-dependent and independent translation, this gene product functions as a general repressor of translation by forming translationally inactive complexes. In vitro and in vivo studies indicate that translation of this mRNA initiates exclusively at a non-AUG (GUG) codon. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
eukaryotic translation initiation factor 4 gamma, 2
, eukaryotic translation initiation factor 4 gamma 2
, Eukaryotic translation initiation factor 4 gamma 2
, aging-associated protein 1
, death-associated protein 5
, eIF-4-gamma 2
, eIF-4G 2
, eIF4G 2
, eukaryotic translation initiation factor 4G-like 1
, eIF4G-related protein NAT1
, novel APOBEC-1 target 1
, translation repressor NAT1
, translation repressor Nat1