Recombinant Human Protein Argonaute-2 (AGO2) Protein (His)

Name: Recombinant Human Protein Argonaute-2 (AGO2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04178P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein Argonaute-2 (AGO2) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UKV8
Target Symbol	AGO2
Synonyms	Ago 2; AGO2_HUMAN; Argonaute 2; argonaute 2; RISC catalytic component; Argonaute RISC catalytic component 2; Argonaute2; CTA-204B4.6; dAgo2; eIF 2C 2; eIF-2C 2; eIF2C 2; Eif2c2; Eukaryotic translation initiation factor 2C 2; Eukaryotic translation initiation factor 2C subunit 2; hAgo2; MGC3183; PAZ Piwi domain protein; PPD; Protein argonaute-2; Protein slicer; Q10; Slicer protein
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	LVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLV
Expression Range	517-818aa
Protein Length	Partial
Mol. Weight	36.1kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions.
Subcellular Location	Cytoplasm, P-body. Nucleus. Note=Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.
Protein Families	Argonaute family, Ago subfamily
Database References	HGNC: 3263 OMIM: 606229 KEGG: hsa:27161 STRING: 9606.ENSP00000220592 UniGene: PMID: 29028450 extracellular vesicles are efficiently internalized by endothelial cells, where the miRNA-Argonaute 2 complexes modulate target gene expression and barrier properties. PMID: 27721445 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 PMID: 28954383 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. PMID: 29017520 Phosphorylation of AGO2 at Ser 387 by Akt3 induces LIMD1 binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6. PMID: 28683311 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. PMID: 29031931 Data show that neuropilin 1 (NRP1) binds extracellular AGO2 (carrying miRNA or not), and internalizes AGO2/miRNA complexes. PMID: 27486976 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 PMID: 28831191 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. PMID: 27924485 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. PMID: 27924486 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-AGOs, that not only block the crucial binding site of the target miRNA but also bind to the protein's active site. PMID: 27924487 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. PMID: 27924488 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. PMID: 27924489 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. PMID: 28388001 The adenovirus major late promoter produces a 31-nucleotide transcriptional start site small RNA (MLP-TSS-sRNA) that retains the 7-methylguanosine (m7G)-cap and is incorporated onto Ago2-containing RNA-induced silencing complexes (RISC) in human adenovirus-37 infected cells. PMID: 28839112 Depletion of AUF1 abolishes the global interaction of miRNAs and AGO2. Single-molecule analysis revealed that AUF1 slowed down assembly of AGO2-let-7b-mRNA complex unexpectedly. AUF1 is a decay-promoting factor influencing multiple steps in AGO2-miRNA-mediated mRNA decay. PMID: 28334781 This lack of 21-3U HCV host factor activity correlated with reduced recruitment of Ago2 to the HCV S1 site. Additional experiments demonstrated strong preference for guanosine at nt 22 of miR-122. Our findings reveal the importance of non-templated 3 miR-122 modifications to its HCV host factor activity, and identify unexpected differences in miRNA requirements for host gene suppression versus RNA virus replication. PMID: 28082397 Low AGO2 expression is associated with melanoma. PMID: 27518285 Altogether, these data suggest that the phosphorylation state of the serine/threonine cluster is important for Argonaute-mRNA interactions. PMID: 28645918 data indicates that the aberrant expression of miR-15b contributes to abnormal placentation by targeting argonaute 2 messenger RNA PMID: 27208409 findings support a model in which an AGO2 phosphorylation cycle stimulated by target engagement regulates miRNA:target interactions to maintain the global efficiency of miRNA-mediated silencing PMID: 28114302 deciphering Ago2:RNA interactions using crosslinking immunoprecipitation coupled with high-throughput sequencing (HITS-CLIP) to generate the first transcriptome-wide map of miR targeting events in human myocardium, detecting 4000 cardiac Ago2 binding sites across 2200 target transcripts PMID: 27418678 AGO2 immunoprecipitation revealed LATS1 as a novel proapoptotic target of miR-21 in T cells. PMID: 28075055 1174 regions within the 45S rRNA transcript that have the ability to form a perfect duplex with position 2-6 (seed sequence) of each microRNA expressed in HEK293T cells. Of these potential AGO2 binding sites, 479 occurred within experimentally verified AGO2-rRNA cross-linking sites. The ability of AGO2 to cross-link to rRNA was almost completely lost in a DICER knock-out cell line. PMID: 27288410 this study analysed binding of miR-122/ Argonaute 2 complexes to two conserved binding sites in the 5' UTR of hepatitis C virus RNA. PMID: 28008821 overactivity of KRAS due to mutation inhibits localization of Ago2 to multivesicular endosomes (MVEs) and decreases Ago2 secretion in exosomes. PMID: 27117408 TP53 regulates miRNA association with AGO2 to remodel the miRNA-mRNA interaction network PMID: 26701625 These results support the notion that the cereblon binding partner AGO2 plays an important role in regulating MM cell growth and survival and AGO2 could be considered as a novel drug target for overcoming IMiD resistance in MM cells. PMID: 27142104 KRAS engages AGO2 to enhance cellular neoplastic transformation. PMID: 26854235 Authors found that target binding of core-RISC starts at the seed region of the guide RNA. After target binding, four distinct reactions followed: target cleavage, transient binding, stable binding, and Argonaute 2 unloading. PMID: 26592935 AGO2 suppression by miR-132 affects the steady state levels of miR-221 and miR-146a, two miRNAs involved in angiogenesis and inflammation, respectively. PMID: 26475020 DIS3L2 interacts with Ago2 and governs target RNA-directed miRNA degradation. PMID: 26809675 MiR-138 suppresses hTERT expression in an AGO2-dependent manner. PMID: 26507454 Knockdown of Ago2 in Huh7 cells and SMMC-7721 cells substantially decreased VEGF expression, whereas the restoration of AGO2 reversed both VEGF expression and secretion. PMID: 25937637 genetic polymorphism in AGO2 may be a risk factor for the advanced lymph node metastasis of NPC in Chinese populations, and AGO2 acts as an oncogene in the development of NPC. PMID: 26545861 Human Argonaute2 (Ago2) possesses a solvated surface pocket that specifically binds adenine nucleobases in the 1 position (t1) of target RNAs. PMID: 26359634 the subcellular distribution of Ago2 occurs in a cell type- and tissue context-dependent manner and may correlate with its various functions in regulation of gene expression PMID: 26699195 HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication PMID: 26451954 GRSF1 participated in the regulation of AGO2 by miR-346, and the middle sequence of miR-346 was vital for the synergy effect of miR-346 and GRSF1. PMID: 26518874 Human AGO2 interacts only with sRNAs (20-30 nt in length), and not with DNA fragments. PMID: 25970378 SERPINE1 mRNA dissociates from the translational repressor proteins Ago2 and TIA-1 upon platelet activation PMID: 25673011 Both argonaute 2 mRNA and protein were upregulated in high-grade when compared to low-grade tumor tissues. Multivariate analysis revealed that argonaute 2 protein expression was independently associated with the overall survival. PMID: 24935600 Targeting of Ago2 to P-bodies and stress granules is separable from its role in RNAi and likely requires dynamic phosphorylation of serine 798. PMID: 26443379 mRNA Targeting to Endoplasmic Reticulum Precedes Ago Protein Interaction and MicroRNA (miRNA)-mediated Translation Repression PMID: 26304123 Ago2 can be SUMOylated in cells by both SUMO1 and SUMO2. SUMOylation occurs primarily at K402, and mutation of the SUMO consensus site surrounding this lysine reduces Ago2-mediated siRNA-induced silencing in a luciferase-based reporter assay. PMID: 26188511 Ago2 overexpression increased the level of miR-16 in cell-secreted MVs, suggesting that Ago2 may facilitate the packaging of secreted miRNAs into MVs. PMID: 25072345 It was demonstrated by deep sequencing that AGO2-processed AgoshRNAs produce RNA effector molecules with more discrete ends than the products of the regular shRNA design. PMID: 25826416 Sumoylation of Ago2 at Lys402 negatively regulates its stability. PMID: 25036361 our results indicate that IRF7 promotes glioma cell invasion and both chemoresistance and radioresistance through AGO2 inhibition PMID: 25680411 a novel mechanism by which AUF1 binding and transfer of microRNA let-7 to AGO2 facilitates let-7-elicited gene silencing. PMID: 26253535

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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