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anti-Human AGO2 Antikörper:
anti-Rat (Rattus) AGO2 Antikörper:
anti-Mouse (Murine) AGO2 Antikörper:
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Human Monoclonal AGO2 Primary Antibody für 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 für 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 für 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 (zeige EIF2C1 Antikörper) 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 (zeige HENMT1 Antikörper) 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 (zeige EIF2C1 Antikörper) or AGO2.
AGO1 (zeige EIF2C1 Antikörper) 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 (zeige NAPA Antikörper) gene, MEMB12.
second layer is activated when the first layer is suppressed because AGO2 is repressed by AGO1 (zeige EIF2C1 Antikörper) via miR403
Phosphorylation of AGO2 at Ser (zeige SIGLEC1 Antikörper) 387 by Akt3 (zeige AKT3 Antikörper) induces LIMD1 (zeige LIMD1 Antikörper) binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6 (zeige DDX6 Antikörper).
AGO2-mediated cleavage of targets is more common than previously thought. This may explain the vital role of endonuclease activity in controlling miRNA-mediated gene regulation.
Data show that neuropilin 1 (NRP1 (zeige NRP1 Antikörper)) binds extracellular AGO2 (carrying miRNA or not), and internalizes AGO2/miRNA complexes.
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 (zeige SPR Antikörper) 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 (zeige MLXIP Antikörper)-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.
Here, we show that partial loss of either APOBEC1 complementation factor (A1CF (zeige A1CF Antikörper)), the RNA-binding cofactor of APOBEC1 (zeige APOBEC1 Antikörper) 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 (zeige MLXIP Antikörper)-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 (zeige SCPEP1 Antikörper)-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 (zeige ATG5 Antikörper)-/- and ATG16 (zeige ATG16L1 Antikörper)-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.
DIS3L2 (zeige DIS3L2 Antikörper) interacts with Ago2 and governs target RNA-directed miRNA degradation.
Results from the liver show that, siRNA targets 3'UTR (zeige UTS2R Antikörper) and the coding sequence (CDs (zeige ABHD5 Antikörper)) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR (zeige UTS2R Antikörper)-targeted siRNA-mediated knockdown are active with the help of Ago1 (zeige EIF2C1 Antikörper) and Ago3 (zeige EIF2C3 Antikörper).
Roquin (zeige RC3H1 Antikörper) also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR (zeige MLXIP Antikörper)-146a, a microRNA that targets Icos (zeige ICOS Antikörper) mRNA.
Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs.
Molecular evolution of AGO2 glutamine (zeige GFPT2 Antikörper)-rich repeat region
Mutation of T1149 or R1158 in the conserved PIWI (zeige PIWIL1 Antikörper) 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 (zeige EIF2C1 Antikörper) 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