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anti-Human AGO2 Antibodies:
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Human Monoclonal AGO2 Primary Antibody for IF, IHC (p) - ABIN565346
Krol, Fiszer, Mykowska, Sobczak, de Mezer, Krzyzosiak: Ribonuclease dicer cleaves triplet repeat hairpins into shorter repeats that silence specific targets. in Molecular cell 2007
Show all 44 Pubmed References
Fruit Fly (Drosophila melanogaster) Polyclonal AGO2 Primary Antibody for ELISA, EM - ABIN252195
Jaglarz, Kloc, Jankowska, Szymanska, Bilinski: Nuage morphogenesis becomes more complex: two translocation pathways and two forms of nuage coexist in Drosophila germline syncytia. in Cell and tissue research 2011
Human Monoclonal AGO2 Primary Antibody for ICC, IF - ABIN2668227
Azuma-Mukai, Oguri, Mituyama, Qian, Asai, Siomi, Siomi: Characterization of endogenous human Argonautes and their miRNA partners in RNA silencing. in Proceedings of the National Academy of Sciences of the United States of America 2008
AGO1, AGO2 and AGO10 promoted anti-TuMV defense in a modular way in various organs, with AGO2 providing a prominent antiviral role in leaves. AGO5, AGO7 and AGO10 had minor effects in leaves.
Base pairing at the 15th nucleotide of a miRNA duplex is important for miRNA sorting in both Arabidopsis AGO1 (show EIF2C1 Antibodies) and AGO2. AGO2 favours miRNA duplexes with no middle mismatches.
Complementation analyses in ago mutant plants revealed that the catalytic residues of AGO1, AGO2, and AGO7 are required to restore the defects of Arabidopsis ago1-25, ago2-1, and zip-1 (AGO7-defective) mutants, respectively.
AGO2 and HEN1 (show HENMT1 Antibodies) participate in the DCL2-mediated antiviral defense to ensure the survival of Turnip crinkle virus-infected plants at high temperature.
This study reveals that miR408, which has a 5'A, regulates its target Plantacyanin through either AGO1 (show EIF2C1 Antibodies) or AGO2.
AGO1 (show EIF2C1 Antibodies) and AGO2 are involved in defense against mutant of Cucumber mosaic virus, which act downstream the biogenesis of viral secondary siRNAs in a nonredundant and cooperative manner.
Results show that AGO2-bound small RNA miR393b( *) targets a Golgi-localized SNARE (show NAPA Antibodies) gene, MEMB12.
second layer is activated when the first layer is suppressed because AGO2 is repressed by AGO1 (show EIF2C1 Antibodies) via miR403
We found a much larger number of microparticles (MPs) results demonstrate that normal RBCs display an innate ability to resist infection by P. falciparum parasite by releasing Ago2-miRNA complexes via microparticles (MPs)into infected RBCs; data suggest that, through release of MPs, mature RBCs present an innate resistance to malaria infection
we describe these two methodologies that we recently used to select a specific compound able to interfere with the AGO2 functional activity and able to improve the retinoic acid-dependent myeloid differentiation of leukemic cells.
Here, we describe the use of SPR (show SPR Antibodies) techniques to study the interaction between Argonaute 2 and small molecular compounds selected by means of high-throughput docking screening.
Since miRNAs' functions are executed exclusively by the Argonaute 2 protein, we therefore describe a protocol for the design of a novel miRNA inhibitor class: antagonists of the miRNA-Argonaute 2 protein complex, so-called anti-miR (show MLXIP Antibodies)-AGOs, that not only block the crucial binding site of the target miRNA but also bind to the protein's active site.
Using our recent work on human AGO2 as an example, we explain the rationale and the workflow of our method in details. This combined approach holds great promise to complement experiments in unraveling the mechanisms of molecular recognition between large, flexible, and complex biomolecules.
Here, we present techniques to kinetically characterize recombinant Argonaute 2-mediated guide and target binding as well as target RNA slicing. We focus on fluorescence-based steady-state and in particular pre-steady-state techniques to unravel mechanistic details. Furthermore, we describe a cleavage assay to analyze Argonaute 2-mediated slicing using radioactively labeled target strands.
This study employed molecular dynamics simulation to investigate the dynamic properties of human Ago2-RNA-duplex system and Ago2-free system to provide further understanding of the molecular mechanism of Ago2-RNA recognition.
WIG1 (show ZMAT3 Antibodies) governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of ACOT7 (show ACOT7 Antibodies) mRNA.
The adenovirus major late promoter produces a 31-nucleotide transcriptional start site small RNA (MLP (show MUC2 Antibodies)-TSS (show RPL38 Antibodies)-sRNA) that retains the 7-methylguanosine (m7G)-cap and is incorporated onto Ago2-containing RNA-induced silencing complexes (RISC (show SCPEP1 Antibodies)) in human adenovirus-37 infected cells.
Depletion of AUF1 (show HNRNPD Antibodies) abolishes the global interaction of miRNAs and AGO2. Single-molecule analysis revealed that AUF1 (show HNRNPD Antibodies) slowed down assembly of AGO2-let-7b-mRNA complex unexpectedly. AUF1 (show HNRNPD Antibodies) is a decay-promoting factor influencing multiple steps in AGO2-miRNA-mediated mRNA decay.
Here, we show that partial loss of either APOBEC1 complementation factor (A1CF (show A1CF Antibodies)), the RNA-binding cofactor of APOBEC1 (show APOBEC1 Antibodies) in RNA editing, or Argonaute 2 (AGO2), a key factor in the biogenesis of certain noncoding RNAs, modulates risk for TGCTs and testicular abnormalities in both parent-of-origin and conventional genetic manners.
This identified Ago2 as a key determinant of quiescence exit in Hematopoietic stem cells.
miR (show MLXIP Antibodies)-9, along with Argonaute proteins (Agos), is localized to the nucleus of quiescent neural stem cells, and manipulating their nuclear/cytoplasmic ratio impacts quiescence.
We propose that RISC (show SCPEP1 Antibodies)-mediated inhibition of specific sets of chromatin regulators is a primary mechanism for preserving embryonic stem cell pluripotency while inhibiting the onset of embryonic developmental programs
Increased AGO2 was detected in autophagy-deficient ATG5 (show ATG5 Antibodies)-/- and ATG16 (show ATG16L1 Antibodies)-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.
DIS3L2 (show DIS3L2 Antibodies) interacts with Ago2 and governs target RNA-directed miRNA degradation.
Results from the liver show that, siRNA targets 3'UTR (show UTS2R Antibodies) and the coding sequence (CDs (show ABHD5 Antibodies)) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR (show UTS2R Antibodies)-targeted siRNA-mediated knockdown are active with the help of Ago1 (show EIF2C1 Antibodies) and Ago3 (show EIF2C3 Antibodies).
Roquin (show RC3H1 Antibodies) also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR (show MLXIP Antibodies)-146a, a microRNA that targets Icos (show ICOS Antibodies) mRNA.
Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs.
Mouse AGO2 binds tighter to miRNA targets than its RNAi cleavage product, even though the cleaved product contains more base pairs. By re-writing the rules for nucleic acid hybridization, Argonautes allow oligonucleotides to serve as specificity determinants with thermodynamic and kinetic properties more typical of RNA-binding proteins than of RNA or DNA.
Molecular evolution of AGO2 glutamine (show GFPT2 Antibodies)-rich repeat region
Mutation of T1149 or R1158 in the conserved PIWI (show PIWIL1 Antibodies) domain causes AGO2 protein instability, but only T1149 affects RNAi activity. Mass spec analysis shows that several proteasome components co-purify with both wildtype and mutant AGO2, and knockdown of two proteasome pathway components results in AGO2 protein accumulation.
We speculate that the repeated evolution of testis specificity in obscura group Ago2 genes, combined with their dynamic turnover and strong signatures of adaptive evolution, may be associated with highly derived roles in the suppression of transposable elements or meiotic drive
We find there are large differences in evolutionary rates and gene turnover between pathways, and that paralogs of Ago2, Ago3, and Piwi/Aub show contrasting rates of evolution after duplication.
Study shows that the Cricket Paralysis virus suppressor of RNA silencing, CrPV-1A but not B2 strongly interfere with the Ago-2-dependent miRNA silencing in Drosophila.
siRNA biogenesis does not stabilize AGO2 in Drosophila.
The results of this study found that mutations in Drosophila Argonaute 2 (Ago2) resulted in exacerbated transposon expression in the brain, progressive and age-dependent memory impairment, and shortened lifespan
analysis of regulation of Argonaute (show EIF2C1 Antibodies) slicer activity by guide RNA 3' end interactions with the N-terminal lobe
two new nuclear roles for Ago-2: one in pre-mRNA splicing and one in transcriptional repression.
Highlighting its role in antiviral defense, fly Ago2 dissociates so slowly from extensively complementary target RNAs that essentially every fully paired target is cleaved. Conversely, mouse AGO2, which mainly mediates miRNA-directed repression, dissociates rapidly and with similar rates for fully paired and seed-matched targets.
This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic, and contains a PAZ domain and a PIWI domain. It may interact with dicer1 and play a role in short-interfering-RNA-mediated gene silencing. Multiple transcript variants encoding different isoforms have been found for this gene.
eukaryotic translation initiation factor 2C, 2
, protein argonaute-2-like
, PAZ Piwi domain protein
, argonaute 2
, eIF-2C 2
, eIF2C 2
, protein argonaute-2
, protein slicer
, golgi ER protein 95 kDa
, Protein slicer
, eukaryotic translation initiation factor 2C, 1
, Piwi/Argonaute family protein meIF2C2
, argonaute RISC catalytic component 2
, eukaryotic translation initiation factor 2C 2
, Eukaryotic translation initiation factor 2C 2
, translation initiation factor eIF2C