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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
Show all 2 Pubmed References
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
PRMT5 directs symmetric arginine dimethylation of AGO2.The N-terminal domain of AGO2 is enriched with arginine-glycine RG/GR repeats, which are methylated by PRMT5.
Data show that Argonaute family protein AGO2 and AGO3 were important for abscisic acid (ABA)-mediated resistance.
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 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 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 or AGO2.
AGO protein has evolved to specialize in antiviral defenses.
AGO1 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 gene, MEMB12.
second layer is activated when the first layer is suppressed because AGO2 is repressed by AGO1 via miR403
L1-5'UTR harbors both sense and antisense promoter activity and a dsRNA-mediated regulation is responsible for L1-5'UTR regulation. Agos proteins and L1-ORF1p were engaged in this process.
we built a computational model that evaluates the importance of base pairing beyond the seed in AGO2-mediated repression. This model suggests that when the seed region is perfectly base paired with the target, then the bps in module-B (nts 12-14) play a decisive role.
results reveal a critical mechanism by which Ser-195 phosphorylation in Rbm38 increases p63 expression by attenuating the association of Rbm38 with the Ago2-miR203 complex.
The results revealed that there were 243 miRNAs and 265 miRNAs in the Ago2 complexes of nucleus and cytoplasm, respectively. The majority of mature miRNAs existed in cytoplasm. The analysis of miRNA targetome from the Ago2 complexes indicated that a lot of mRNAs with high expression level existed in nucleus.
all research findings suggested that CASC7 inhibited the progression of glioma via regulating Wnt/beta-catenin signaling pathway
Our finding reveals a novel function of AGO2 acetylation in increasing oncogenic miR-19b biogenesis and suggests that modulation of AGO2 acetylation has potential clinical implications.
P38 activation repressed the cooperation of TTP with Ago2, thus ensuring that ARE-mRNA does not associate with processing bodies and remains stable.
IFN-gamma and TNF induce a stable cell cycle arrest of cancer cells that is accompanied by a fast nuclear Ago2 translocation and repression of Ago2-regulated cell cycle control genes. As Ago2 downregulation impairs cytokine-induced growth regulation, Ago2 may contribute to tissue homeostasis in human cancers.
We observed that the designed ss-miR-216b mimics engaged AGO2 to promote the silencing of KRAS. We also tested a new delivery strategy based on the use of palmityl-oleyl-phosphatidylcholine (POPC) liposomes functionalized with ss-miR-216b conjugated with two palmityl chains and a lipid-modified cell penetrating peptide . These versatile nanoparticles suppressed oncogenic KRAS in pancreatic ductal adenocarcinoma cells
Here we show that biotin-labelled miR-34a can be loaded to AGO2, and AGO2 immunoprecipitation can pulldown biotinylated miR-34a (Bio-miR pulldown). RNA-sequencing (RNA-seq) of the Bio-miR pulldown RNAs efficiently identified miR-34a mRNA targets, which could be verified with luciferase assays
extracellular vesicles are efficiently internalized by endothelial cells, where the miRNA-Argonaute 2 complexes modulate target gene expression and barrier properties.
CASC7 expression was significantly decreased in colorectal cancer (CRC) tissues and CRC cell lines; CASC7 overexpression could inhibit cell viability, migration and invasion, and promote apoptosis in CRC cells
A dual role of the association between AGO2 and ERbeta in luminal-like breast cancer cells in the nucleus and the cytoplasm, for the regulation of gene expression at both the transcriptional and post-transcriptional level.
Decreased argonaute 2 and dicer1 in peripheral blood mononuclear cells from War Veterans with post-traumatic stress disorder leads to diminished miRNA resulting in elevated inflammation.
Phosphorylation of AGO2 at Ser 387 by Akt3 induces LIMD1 binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6.
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) 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 techniques to study the interaction between Argonaute 2 and small molecular compounds selected by means of high-throughput docking screening.
The microRNA effector protein AGO2 is predominantly expressed as an alternative isoform that encodes a truncated protein lacking all of the known essential domains. Full-length Ago2 was lowly expressed in maturing mouse oocytes. Reintroduction of full-length AGO2 together with an exogenous microRNA in either mouse or frog oocytes restored translational repression of a target reporter.
We proved that this defect is cell autonomous and can be rescued by both a catalytically active and an inactive Ago2, but not by Ago2 deprived of its RNA binding capacity or by Ago1 overexpression. Overall, our results suggest a role for AGO2 in stem cell differentiation
hepatic Ago2-mediated RNA silencing has a role in regulating energy metabolism linked to AMPK activation and obesity-associated pathophysiology
Here, we show that partial loss of either APOBEC1 complementation factor (A1CF), the RNA-binding cofactor of APOBEC1 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-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-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-/- and ATG16-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.
DIS3L2 interacts with Ago2 and governs target RNA-directed miRNA degradation.
Results from the liver show that, siRNA targets 3'UTR and the coding sequence (CDs) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR-targeted siRNA-mediated knockdown are active with the help of Ago1 and Ago3.
Roquin also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR-146a, a microRNA that targets Icos mRNA.
mRNA Targeting to Endoplasmic Reticulum Precedes Ago Protein Interaction and MicroRNA (miRNA)-mediated Translation Repression
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.
Mouse Ago2 can be expressed as a fusion protein with the maltose binding protein in a soluble and enzymatically active form, without requiring coexpression with chaperones and cleave the complementary RNA in absence of other cellular factors.
This study identifies the targeting of Ago2 by miR-184 as an essential component of the compensatory response to regulate proliferation according to insulin sensitivity.
study identifies Fkbp4 and Fkbp5 as novel components of the Ago2 RISC loading complex
Insights into the role of Ago2 in the systemic release of proteins from beta-cells.
In mouse cells, Ago2 stability declined in Dicer-knockout cells & was rescued by proteasome blockade or introduction of either Dicer plasmid or Dicer-independent miRNA constructs.
Cricket paralysis virus protein CrPV-1A comprises a BC-box motif to recruit an E3 ubiquitin ligase for Ago-2 degradation.
Conserved association of Argonaute 1 and 2 proteins with miRNA and siRNA pathways throughout insect evolution, from cockroaches to flies.
Results provide evidence for an Ago2-interaction network participating in dosage compensation in drosophila.
findings reveal coordination of AGO2 and LaminB function to dictate genome architecture and thereby regulate gene expression
Molecular evolution of AGO2 glutamine-rich repeat region
Mutation of T1149 or R1158 in the conserved PIWI 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 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.
Nora virus VP1 and the viral suppressor of RNAi of Cricket paralysis virus (1A) antagonized Argonaute-2 (AGO2) Slicer activity of RNA induced silencing complexes pre-loaded with a methylated single-stranded guide strand.
the key RNAi components Dicer 2 (DCR2) and Argonaute 2 (AGO2) associate with chromatin (with a strong preference for euchromatic, transcriptionally active, loci) and interact with the core transcription machinery
Data show that AGO2 interacts physically with CTCF and CP190, and depletion of either CTCF or CP190 results in genome-wide loss of AGO2 chromatin association.
GRR variation does not modulate an essential function of Ago2 and the amino-terminal domain of Ago2 is subject to rapid evolution
Data suggest that recent independent selective sweeps in AGO2 have reduced genetic variation across a region of more than 50 kbp in Drosophila melanogaster, D. simulans, and D. yakuba.
Mutation of AGO2 or piwi increases silencing at piRNA clusters corresponding to an increase of HP1 association.
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