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Validated All-in-One™ qPCR Primer for AGO2(NM_012154.4) Search again
Product ID:
HQP098738
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
CASC7, EIF2C2, LESKRES, LINC00980, PPD, Q10
Gene Description:
argonaute RISC catalytic component 2
Target Gene Accession:
NM_012154.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
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. [provided by RefSeq].
Gene References into function
- responsible for messenger RNA cleavage activity; evidence supports a model in which Argonaute contributes "Slicer" activity to RISC, providing the catalytic engine for RNAi
- Argonaute proteins catalyze mRNA cleavage within RNA-Induced Silencing Complex
- Argonaute 2, a key component of RISC, is not randomly distributed but concentrates in mRNA decay centres that are known as cytoplasmic bodies.
- Activity of siRNA duplexes containing full 2'-OMe substitutions in the sense strand is mediated by the RNA-induced silencing complex and that strand-specific loading to hAgo2 may be modulated through selective incorporation of these modifications.
- miRNA loading complex (miRLC) is formed by Ago2 and Dicer prior to their encounter with pre-miRNA.
- Here, we show that the human slicer Argonaute2 (HsAgo2), but not HsAgo1, functions in RNAi in the early divergent protozoan Trypanosoma brucei, thus mimicking the situation in mammalian cells
- AGO1 and AGO2 associate with promoter DNA in cells treated with antigene RNAs (agRNAs), and inhibiting expression of AGO1 or AGO2 reverses transcriptional and post-transcriptional silencing.
- give a quantitative account of the Argonaute protein localization and dynamics in living cells in different cellular states
- A crosslinking-coupled affinity purification method was used to isolate TNF-alpha AU-rich element-associated proteins: two microRNP-related proteins, FXR1 and AGO2 were found that associate during translation activation.
- Ago2 represses the initiation of mRNA translation by binding to the m(7)G cap of mRNA targets, thus likely precluding the recruitment of eIF4E
- The action of RNA-induced silencing complex (RISC) requires the endonucleolytic slicer activity of Argonaute2 (Ago2)
- Local widening of the duplex formed by the siRNA guide strand and the targeted region of mRNA is a possible reason for the intolerance of human Ago2, the RISC endonuclease, toward internal mismatch pairs involving native or chemically modified RNA.
- Results describe a repetitive motif within Tas3, termed the 'Argonaute hook', that is conserved from yeast to humans and binds Ago1 and 2 through their PIWI domains in vitro and in vivo.
- Data show that Argonaute1 and 2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities, and that the putative RNA-binding protein RBM4 is required for microRNA-guided gene regulation.
- Ago2, Dicer, and TRBP comprise the RISC-loading complex (RLC) and assembles spontaneously in vitro from purified components
- These present data demonstrate that siAgo2 inhibited indispensable events of angiogenesis in vitro.
- The results suggest a potential regulatory mechanism for RNA silencing acting through Ago2 serine-387 phosphorylation mediated by the p38 MAPK pathway.
- Ectopic expression of the Argonaute-2 (Ago2, eIF2C2) dramatically enhances RNA interference specifically for mRNA targets with perfectly matched binding sites.
- findings identify hydroxylation as a post-translational modification important for Ago2 stability and effective RNA interference
- The specificity of RNA interference depends on the concentration of Ago1, Ago3, and Ago4 relative to Ago2.
- Ago2 is regulated at both the transcriptional and posttranslational level, and Ago2 and enhanced micro-RNA activity is seen in the tumorigenic progression of breast cancer cell lines.
- Data show that siRNA transfection induces up-regulated expression of both GW182, a key P-body component, and Ago2, indicating that P-body localization and interaction with GW182 and Ago2 are important in siRNA-mediated RNAi.
- plays a roll in processes of tumor angiogenesis.
- Mutant Ago2 protein containing 6 point mutations (G32W, F128L, R196Q, P458S, T741A, S752G) failed to accumulate in P-bodies.
- Study demonstrates that Imp8 is required for the recruitment of Ago protein complexes to a large set of Ago2-associated target mRNAs, allowing for efficient and specific gene silencing.
